CAH2_HUMAN
ID CAH2_HUMAN Reviewed; 260 AA.
AC P00918; B2R7G8; Q6FI12; Q96ET9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 260.
DE RecName: Full=Carbonic anhydrase 2;
DE EC=4.2.1.1 {ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:9398308};
DE AltName: Full=Carbonate dehydratase II;
DE AltName: Full=Carbonic anhydrase C;
DE Short=CAC;
DE AltName: Full=Carbonic anhydrase II;
DE Short=CA-II;
DE AltName: Full=Cyanamide hydratase CA2 {ECO:0000305};
DE EC=4.2.1.69 {ECO:0000269|PubMed:10550681};
GN Name=CA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3108857; DOI=10.1093/nar/15.11.4687;
RA Montgomery J.C., Venta P.J., Tashian R.E., Hewett-Emmett D.;
RT "Nucleotide sequence of human liver carbonic anhydrase II cDNA.";
RL Nucleic Acids Res. 15:4687-4687(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3121496; DOI=10.1016/0888-7543(87)90008-5;
RA Murakami H., Marelich G.P., Grubb J.H., Kyle J.W., Sly W.S.;
RT "Cloning, expression, and sequence homologies of cDNA for human carbonic
RT anhydrase II.";
RL Genomics 1:159-166(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-260, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT SER-2.
RX PubMed=4207120; DOI=10.1016/s0021-9258(19)42734-8;
RA Lin K.-T.D., Deutsch H.F.;
RT "Human carbonic anhydrases. XII. The complete primary structure of the C
RT isozyme.";
RL J. Biol. Chem. 249:2329-2337(1974).
RN [8]
RP PROTEIN SEQUENCE OF 2-260.
RX PubMed=823150; DOI=10.1016/s0021-9258(17)33081-8;
RA Henderson L.E., Henriksson D., Nyman P.O.;
RT "Primary structure of human carbonic anhydrase C.";
RL J. Biol. Chem. 251:5457-5463(1976).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=3000449; DOI=10.1016/0167-4781(85)90006-5;
RA Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.;
RT "Comparison of the 5' regions of human and mouse carbonic anhydrase II
RT genes and identification of possible regulatory elements.";
RL Biochim. Biophys. Acta 826:195-201(1985).
RN [10]
RP INTERACTION WITH SLC4A4.
RX PubMed=14567693; DOI=10.1021/bi0353124;
RA Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
RT "Direct extracellular interaction between carbonic anhydrase IV and the
RT human NBC1 sodium/bicarbonate co-transporter.";
RL Biochemistry 42:12321-12329(2003).
RN [11]
RP INTERACTION WITH SLC4A7.
RX PubMed=14736710; DOI=10.1152/ajpcell.00382.2003;
RA Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.;
RT "Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase
RT II and PKA.";
RL Am. J. Physiol. 286:C1423-C1433(2004).
RN [12]
RP INTERACTION WITH SLC4A4.
RX PubMed=15218065; DOI=10.1113/jphysiol.2004.065110;
RA Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I.,
RA Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
RT "Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal
RT tubule cells.";
RL J. Physiol. (Lond.) 559:55-65(2004).
RN [13]
RP FUNCTION, INTERACTION WITH SLC26A6, AND SUBCELLULAR LOCATION.
RX PubMed=15990874; DOI=10.1038/sj.emboj.7600736;
RA Alvarez B.V., Vilas G.L., Casey J.R.;
RT "Metabolon disruption: a mechanism that regulates bicarbonate transport.";
RL EMBO J. 24:2499-2511(2005).
RN [14]
RP ACTIVITY REGULATION.
RX PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
RA Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
RA Supuran C.T.;
RT "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray
RT crystal structure of the antiviral drug foscarnet complexed to human
RT carbonic anhydrase I.";
RL Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
RN [15]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=18618712; DOI=10.1002/prot.22144;
RA Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
RA Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
RT "Crystal structure of human carbonic anhydrase XIII and its complex with
RT the inhibitor acetazolamide.";
RL Proteins 74:164-175(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4621826; DOI=10.1038/newbio235131a0;
RA Liljas A., Kannan K.K., Bergsten P.-C., Waara I., Fridborg K.,
RA Strandberg B., Carlbom U., Jaerup L., Loevgren S., Petef M.;
RT "Crystal structure of human carbonic anhydrase C.";
RL Nature New Biol. 235:131-137(1972).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION.
RX PubMed=3151019; DOI=10.1002/prot.340040406;
RA Eriksson A.E., Jones T.A., Liljas A.;
RT "Refined structure of human carbonic anhydrase II at 2.0-A resolution.";
RL Proteins 4:274-282(1988).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP INHIBITORS.
RX PubMed=3151020; DOI=10.1002/prot.340040407;
RA Eriksson A.E., Kylsten P.M., Jones T.A., Liljas A.;
RT "Crystallographic studies of inhibitor binding sites in human carbonic
RT anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at high
RT pH.";
RL Proteins 4:283-293(1988).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT SER-199 IN COMPLEX WITH
RP ZINC ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-199, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1909891; DOI=10.1021/bi00102a005;
RA Krebs J.F., Fierke C.A., Alexander R.S., Christianson D.W.;
RT "Conformational mobility of His-64 in the Thr-200TO: human carbonic
RT anhydrase II.";
RL Biochemistry 30:9153-9160(1991).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS PHE-142; TYR-142 AND
RP HIS-142 IN COMPLEX WITH INHIBITORS, AND MUTAGENESIS OF VAL-142.
RX PubMed=1932029; DOI=10.1021/bi00110a008;
RA Alexander R.S., Nair S.K., Christianson D.W.;
RT "Engineering the hydrophobic pocket of carbonic anhydrase II.";
RL Biochemistry 30:11064-11072(1991).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ALA-121, FUNCTION,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF VAL-121, AND ACTIVITY REGULATION.
RX PubMed=1910042; DOI=10.1016/s0021-9258(19)47376-6;
RA Nair S.K., Calderone T.L., Christianson D.W., Fierke C.A.;
RT "Altering the mouth of a hydrophobic pocket. Structure and kinetics of
RT human carbonic anhydrase II mutants at residue Val-121.";
RL J. Biol. Chem. 266:17320-17325(1991).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP INHIBITORS, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1336460; DOI=10.1111/j.1432-1033.1992.tb17490.x;
RA Mangani S., Haakansson K.;
RT "Crystallographic studies of the binding of protonated and unprotonated
RT inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate
RT anions.";
RL Eur. J. Biochem. 210:867-871(1992).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP INHIBITORS.
RX PubMed=1433293; DOI=10.1016/0022-2836(92)90531-n;
RA Haakansson K., Carlsson M., Svensson L.A., Liljas A.;
RT "Structure of native and apo carbonic anhydrase II and structure of some of
RT its anion-ligand complexes.";
RL J. Mol. Biol. 227:1192-1204(1992).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH COBALT ION AND
RP BICARBONATE.
RX PubMed=1474587; DOI=10.1016/0022-2836(92)90327-g;
RA Haakansson K., Wehnert A.;
RT "Structure of cobalt carbonic anhydrase complexed with bicarbonate.";
RL J. Mol. Biol. 228:1212-1218(1992).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT CYS-94 IN COMPLEX WITH
RP ZINC ION, AND MUTAGENESIS OF HIS-94.
RX PubMed=8431430; DOI=10.1021/bi00057a015;
RA Alexander R.S., Kiefer L.L., Fierke C.A., Christianson D.W.;
RT "Engineering the zinc binding site of human carbonic anhydrase II:
RT structure of the His-94-->Cys apoenzyme in a new crystalline form.";
RL Biochemistry 32:1510-1518(1993).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-197; GLU-197; HIS-197
RP AND ARG-197, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-197.
RX PubMed=8485129; DOI=10.1021/bi00068a005;
RA Nair S.K., Christianson D.W.;
RT "Structural consequences of hydrophilic amino acid substitutions in the
RT hydrophobic pocket of human carbonic anhydrase II.";
RL Biochemistry 32:4506-4514(1993).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT CYS-198 IN COMPLEX WITH
RP ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-198.
RX PubMed=8399159; DOI=10.1021/bi00089a005;
RA Ippolito J.A., Christianson D.W.;
RT "Structure of an engineered His3Cys zinc binding site in human carbonic
RT anhydrase II.";
RL Biochemistry 32:9901-9905(1993).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-201 IN COMPLEX WITH
RP ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PRO-201.
RX PubMed=8218160; DOI=10.1021/bi00092a003;
RA Tweedy N.B., Nair S.K., Paterno S.A., Fierke C.A., Christianson D.W.;
RT "Structure and energetics of a non-proline cis-peptidyl linkage in a
RT proline-202-->alanine carbonic anhydrase II variant.";
RL Biochemistry 32:10944-10949(1993).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP INHIBITORS.
RX PubMed=8482389; DOI=10.1016/0014-5793(93)81565-h;
RA Joensson B.M., Haakansson K., Liljas A.;
RT "The structure of human carbonic anhydrase II in complex with bromide and
RT azide.";
RL FEBS Lett. 322:186-190(1993).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT VAL-198 IN COMPLEX WITH
RP ZINC ION AND INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP THR-198, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8262987; DOI=10.1016/s0021-9258(19)74269-0;
RA Krebs J.F., Ippolito J.A., Christianson D.W., Fierke C.A.;
RT "Structural and functional importance of a conserved hydrogen bond network
RT in human carbonic anhydrase II.";
RL J. Biol. Chem. 268:27458-27466(1993).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC
RP ION.
RX PubMed=8331673; DOI=10.1006/jmbi.1993.1365;
RA Mangani S., Liljas A.;
RT "Crystal structure of the complex between human carbonic anhydrase II and
RT the aromatic inhibitor 1,2,4-triazole.";
RL J. Mol. Biol. 232:9-14(1993).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT HIS-199 IN COMPLEX WITH
RP BICARBONATE AND ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP THR-199.
RX PubMed=8451242; DOI=10.1002/prot.340150110;
RA Xue Y., Vidgren J., Svensson L.A., Liljas A., Jonsson B.H., Lindskog S.;
RT "Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and
RT its complex with the substrate, HCO3-.";
RL Proteins 15:80-87(1993).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS IN COMPLEX WITH
RP BICARBONATE AND ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP GLU-106 AND THR-198.
RX PubMed=7901850; DOI=10.1002/prot.340170112;
RA Xue Y., Liljas A., Jonsson B.H., Lindskog S.;
RT "Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond
RT network in human carbonic anhydrase II.";
RL Proteins 17:93-106(1993).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT; COPPER;
RP NICKEL AND MANGANESE IONS.
RX PubMed=15299481; DOI=10.1107/s0907444993008790;
RA Haakansson K., Wehnert A., Liljas A.;
RT "X-ray analysis of metal-substituted human carbonic anhydrase II
RT derivatives.";
RL Acta Crystallogr. D 50:93-100(1994).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) MUTANT GLN-106 IN COMPLEX WITH THE
RP INHIBITOR ACETATE, AND MUTAGENESIS OF GLU-106.
RX PubMed=15299482; DOI=10.1107/s0907444993009667;
RA Haakansson K., Briand C., Zaitsev V., Xue Y., Liljas A.;
RT "Wild-type and E106Q mutant carbonic anhydrase complexed with acetate.";
RL Acta Crystallogr. D 50:101-104(1994).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-259 OF MUTANTS ALA-94; CYS-94;
RP CYS-96; CYS-119 AND ASP-119 IN COMPLEX WITH ZINC ION.
RX PubMed=7803386; DOI=10.1021/bi00255a004;
RA Ippolito J.A., Christianson D.W.;
RT "Structural consequences of redesigning a protein-zinc binding site.";
RL Biochemistry 33:15241-15249(1994).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP TRIFLUOROMETHANE SULFONAMIDE.
RX PubMed=8070585; DOI=10.1016/0014-5793(94)00798-5;
RA Haakansson K., Liljas A.;
RT "The structure of a complex between carbonic anhydrase II and a new
RT inhibitor, trifluoromethane sulphonamide.";
RL FEBS Lett. 350:319-322(1994).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=8142888; DOI=10.1002/pro.5560030115;
RA Smith G.M., Alexander R.S., Christianson D.W., McKeever B.M.,
RA Ponticello G.S., Springer J.P., Randall W.C., Baldwin J.J., Habecker C.N.;
RT "Positions of His-64 and a bound water in human carbonic anhydrase II upon
RT binding three structurally related inhibitors.";
RL Protein Sci. 3:118-125(1994).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ARG-197; ASP-197 AND
RP PHE-197 IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
RX PubMed=7696263; DOI=10.1021/bi00012a016;
RA Nair S.K., Krebs J.F., Christianson D.W., Fierke C.A.;
RT "Structural basis of inhibitor affinity to variants of human carbonic
RT anhydrase II.";
RL Biochemistry 34:3981-3989(1995).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=7608893; DOI=10.1021/jm00013a004;
RA Boriack P.A., Christianson D.W., Kingery-Wood J., Whitesides G.M.;
RT "Secondary interactions significantly removed from the sulfonamide binding
RT pocket of carbonic anhydrase II influence inhibitor binding constants.";
RL J. Med. Chem. 38:2286-2291(1995).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANTS ASP-198; GLU-198 AND
RP HIS-198 IN COMPLEX WITH ZINC ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF THR-198, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7761440; DOI=10.1073/pnas.92.11.5017;
RA Ippolito J.A., Baird T.T. Jr., McGee S.A., Christianson D.W., Fierke C.A.;
RT "Structure-assisted redesign of a protein-zinc-binding site with femtomolar
RT affinity.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5017-5021(1995).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF THE MUTANT GLN-117 IN COMPLEX
RP WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, FUNCTION, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF GLU-117.
RX PubMed=8639494; DOI=10.1021/bi9526692;
RA Huang C.C., Lesburg C.A., Kiefer L.L., Fierke C.A., Christianson D.W.;
RT "Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically
RT diminishes catalysis and enhances metal equilibration kinetics in carbonic
RT anhydrase II.";
RL Biochemistry 35:3439-3446(1996).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS GLY-65; HIS-65; LEU-65;
RP PHE-65; SER-65 AND THR-65 IN COMPLEX WITH ZINC ION.
RX PubMed=8987974; DOI=10.1021/bi9617872;
RA Scolnick L.R., Christianson D.W.;
RT "X-ray crystallographic studies of alanine-65 variants of carbonic
RT anhydrase II reveal the structural basis of compromised proton transfer in
RT catalysis.";
RL Biochemistry 35:16429-16434(1996).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP DANSYLAMIDE.
RX PubMed=8557623; DOI=10.1074/jbc.271.2.1003;
RA Nair S.K., Elbaum D., Christianson D.W.;
RT "Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-
RT naphthalene sulfonamide to human carbonic anhydrase II. Implications for
RT the development of a zinc biosensor.";
RL J. Biol. Chem. 271:1003-1007(1996).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THE ACTIVATOR
RP HISTAMINE, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=9265618; DOI=10.1021/bi970760v;
RA Briganti F., Mangani S., Orioli P., Scozzafava A., Vernaglione G.,
RA Supuran C.T.;
RT "Carbonic anhydrase activators: X-ray crystallographic and spectroscopic
RT investigations for the interaction of isozymes I and II with histamine.";
RL Biochemistry 36:10384-10392(1997).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS ASN-94; ASN-119 AND
RP GLN-119 IN COMPLEX WITH ZINC ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF HIS-94 AND HIS-119, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9398308; DOI=10.1021/bi971296x;
RA Lesburg C.A., Huang C., Christianson D.W., Fierke C.A.;
RT "Histidine --> carboxamide ligand substitutions in the zinc binding site of
RT carbonic anhydrase II alter metal coordination geometry but retain
RT catalytic activity.";
RL Biochemistry 36:15780-15791(1997).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP BRINZOLAMIDE.
RX PubMed=9541386; DOI=10.1002/pro.5560070303;
RA Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A.,
RA Dean T., Laipis P., Silverman D.N., Christianson D.W.;
RT "Structures of murine carbonic anhydrase IV and human carbonic anhydrase II
RT complexed with brinzolamide: molecular basis of isozyme-drug
RT discrimination.";
RL Protein Sci. 7:556-563(1998).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SULFONAMIDE
RP INHIBITORS AND ZINC ION.
RX PubMed=9865942; DOI=10.1002/pro.5560071201;
RA Boriack-Sjodin P.A., Zeitlin S., Chen H.H., Crenshaw L., Gross S.,
RA Dantanarayana A., Delgado P., May J.A., Dean T., Christianson D.W.;
RT "Structural analysis of inhibitor binding to human carbonic anhydrase II.";
RL Protein Sci. 7:2483-2489(1998).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYANAMIDE AND
RP SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10550681; DOI=10.1007/s007750050375;
RA Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.;
RT "Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking
RT the physiological reaction?";
RL J. Biol. Inorg. Chem. 4:528-536(1999).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CYANAMIDE, AND
RP FUNCTION.
RX PubMed=11015219; DOI=10.1021/bi000937c;
RA Guerri A., Briganti F., Scozzafava A., Supuran C.T., Mangani S.;
RT "Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II
RT suggested by cryogenic X-ray diffraction.";
RL Biochemistry 39:12391-12397(2000).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS ILE-93/MET-95/VAL-97 AND
RP SER-93/LEU-95/MET-97 IN COMPLEX WITH COBALT; COPPER AND ZINC IONS.
RX PubMed=11076507; DOI=10.1021/bi001649j;
RA Cox J.D., Hunt J.A., Compher K.M., Fierke C.A., Christianson D.W.;
RT "Structural influence of hydrophobic core residues on metal binding and
RT specificity in carbonic anhydrase II.";
RL Biochemistry 39:13687-13694(2000).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH
RP 4-METHYLIMIDAZOLE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-64.
RX PubMed=11327835; DOI=10.1021/bi002295z;
RA Duda D., Tu C., Qian M., Laipis P., Agbandje-McKenna M., Silverman D.N.,
RA McKenna R.;
RT "Structural and kinetic analysis of the chemical rescue of the proton
RT transfer function of carbonic anhydrase II.";
RL Biochemistry 40:1741-1748(2001).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT VAL-130 IN COMPLEX WITH
RP FLUOROAROMATIC INHIBITORS.
RX PubMed=11572683; DOI=10.1021/ja011034p;
RA Kim C.Y., Chandra P.P., Jain A., Christianson D.W.;
RT "Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the
RT crystal lattice of human carbonic anhydrase II.";
RL J. Am. Chem. Soc. 123:9620-9627(2001).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR SUGAR
RP SULFAMATE RWJ-37497, AND ACTIVITY REGULATION.
RX PubMed=11802772; DOI=10.1042/0264-6021:3610437;
RA Recacha R., Costanzo M.J., Maryanoff B.E., Chattopadhyay D.;
RT "Crystal structure of human carbonic anhydrase II complexed with an anti-
RT convulsant sugar sulphamate.";
RL Biochem. J. 361:437-441(2002).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF THE MUTANT PRO-198/SER-205 IN
RP COMPLEX WITH BICARBONATE AND INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF THR-198.
RX PubMed=12056894; DOI=10.1021/bi020053o;
RA Huang S., Sjoeblom B., Sauer-Eriksson A.E., Jonsson B.H.;
RT "Organization of an efficient carbonic anhydrase: implications for the
RT mechanism based on structure-function studies of a T199P/C206S mutant.";
RL Biochemistry 41:7628-7635(2002).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF THE MUTANT HIS-7, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-7.
RX PubMed=12171926; DOI=10.1074/jbc.m205791200;
RA Tu C., Qian M., An H., Wadhwa N.R., Duda D., Yoshioka C., Pathak Y.,
RA McKenna R., Laipis P.J., Silverman D.N.;
RT "Kinetic analysis of multiple proton shuttles in the active site of human
RT carbonic anhydrase.";
RL J. Biol. Chem. 277:38870-38876(2002).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP FUNCTION.
RX PubMed=11831900; DOI=10.1021/jm010163d;
RA Kim C.Y., Whittington D.A., Chang J.S., Liao J., May J.A.,
RA Christianson D.W.;
RT "Structural aspects of isozyme selectivity in the binding of inhibitors to
RT carbonic anhydrases II and IV.";
RL J. Med. Chem. 45:888-893(2002).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=12166932; DOI=10.1021/jm011112j;
RA Grueneberg S., Stubbs M.T., Klebe G.;
RT "Successful virtual screening for novel inhibitors of human carbonic
RT anhydrase: strategy and experimental confirmation.";
RL J. Med. Chem. 45:3588-3602(2002).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=11818565; DOI=10.1073/pnas.032673399;
RA Grzybowski B.A., Ishchenko A.V., Kim C.Y., Topalov G., Chapman R.,
RA Christianson D.W., Whitesides G.M., Shakhnovich E.I.;
RT "Combinatorial computational method gives new picomolar ligands for a known
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1270-1273(2002).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH
RP THE INHIBITOR 4-METHYLIMIDAZOLE AND ZINC ION.
RX PubMed=12499545; DOI=10.1107/s0907444902019455;
RA Duda D., Govindasamy L., Agbandje-McKenna M., Tu C., Silverman D.N.,
RA McKenna R.;
RT "The refined atomic structure of carbonic anhydrase II at 1.05 A
RT resolution: implications of chemical rescue of proton transfer.";
RL Acta Crystallogr. D 59:93-104(2003).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=14736236; DOI=10.1021/jm030912m;
RA Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A.,
RA Klebe G.;
RT "Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective
RT celecoxib: new pharmacological opportunities due to related binding site
RT recognition.";
RL J. Med. Chem. 47:550-557(2004).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THE ANTI-CANCER
RP AGENT 667-COUMATE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15453828; DOI=10.1042/bj20041037;
RA Lloyd M.D., Pederick R.L., Natesh R., Woo L.W., Purohit A., Reed M.J.,
RA Acharya K.R., Potter B.V.;
RT "Crystal structure of human carbonic anhydrase II at 1.95 A resolution in
RT complex with 667-coumate, a novel anti-cancer agent.";
RL Biochem. J. 385:715-720(2005).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), MUTAGENESIS OF ASN-62; HIS-64 AND
RP ASN-67, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15667203; DOI=10.1021/bi0480279;
RA Fisher Z., Hernandez Prada J.A., Tu C., Duda D., Yoshioka C., An H.,
RA Govindasamy L., Silverman D.N., McKenna R.;
RT "Structural and kinetic characterization of active-site histidine as a
RT proton shuttle in catalysis by human carbonic anhydrase II.";
RL Biochemistry 44:1097-1105(2005).
RN [66]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH DUAL
RP AROMATASE-STEROID SULFATASE INHIBITORS, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15865431; DOI=10.1021/bi047692e;
RA Lloyd M.D., Thiyagarajan N., Ho Y.T., Woo L.W., Sutcliffe O.B., Purohit A.,
RA Reed M.J., Acharya K.R., Potter B.V.;
RT "First crystal structures of human carbonic anhydrase II in complex with
RT dual aromatase-steroid sulfatase inhibitors.";
RL Biochemistry 44:6858-6866(2005).
RN [67]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACTIVATOR
RP L-HISTIDINE, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=16214338; DOI=10.1016/j.bmcl.2005.08.069;
RA Temperini C., Scozzafava A., Puccetti L., Supuran C.T.;
RT "Carbonic anhydrase activators: X-ray crystal structure of the adduct of
RT human isozyme II with L-histidine as a platform for the design of stronger
RT activators.";
RL Bioorg. Med. Chem. Lett. 15:5136-5141(2005).
RN [68]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX PubMed=16134940; DOI=10.1021/jm050333c;
RA Menchise V., De Simone G., Alterio V., Di Fiore A., Pedone C.,
RA Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: stacking with Phe131 determines active site
RT binding region of inhibitors as exemplified by the X-ray crystal structure
RT of a membrane-impermeant antitumor sulfonamide complexed with isozyme II.";
RL J. Med. Chem. 48:5721-5727(2005).
RN [69]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF HIS-64 AND THR-199.
RX PubMed=16106378; DOI=10.1002/prot.20615;
RA Bhatt D., Tu C., Fisher S.Z., Hernandez Prada J.A., McKenna R.,
RA Silverman D.N.;
RT "Proton transfer in a Thr200His mutant of human carbonic anhydrase II.";
RL Proteins 61:239-245(2005).
RN [70]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX PubMed=16511248; DOI=10.1107/s1744309105038248;
RA Budayova-Spano M., Fisher S.Z., Dauvergne M.T., Agbandje-McKenna M.,
RA Silverman D.N., Myles D.A., McKenna R.;
RT "Production and X-ray crystallographic analysis of fully deuterated human
RT carbonic anhydrase II.";
RL Acta Crystallogr. F 62:6-9(2006).
RN [71]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=16820676; DOI=10.1107/s1744309106020446;
RA Fisher S.Z., Govindasamy L., Boyle N., Agbandje-McKenna M., Silverman D.N.,
RA Blackburn G.M., McKenna R.;
RT "X-ray crystallographic studies reveal that the incorporation of spacer
RT groups in carbonic anhydrase inhibitors causes alternate binding modes.";
RL Acta Crystallogr. F 62:618-622(2006).
RN [72]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS
RP VALDECOXIB AND CELECOXIB, AND ACTIVITY REGULATION.
RX PubMed=16290146; DOI=10.1016/j.bmcl.2005.09.040;
RA Di Fiore A., Pedone C., D'Ambrosio K., Scozzafava A., De Simone G.,
RA Supuran C.T.;
RT "Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site
RT region of the human isoform II as compared to the structurally related
RT cyclooxygenase II 'selective' inhibitor celecoxib.";
RL Bioorg. Med. Chem. Lett. 16:437-442(2006).
RN [73]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N-HYDROXYUREA, AND
RP ACTIVITY REGULATION.
RX PubMed=16759856; DOI=10.1016/j.bmcl.2006.05.068;
RA Temperini C., Innocenti A., Scozzafava A., Supuran C.T.;
RT "N-hydroxyurea -- a versatile zinc binding function in the design of
RT metalloenzyme inhibitors.";
RL Bioorg. Med. Chem. Lett. 16:4316-4320(2006).
RN [74]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=17000110; DOI=10.1016/j.bmcl.2006.09.022;
RA Menchise V., De Simone G., Di Fiore A., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: X-ray crystallographic studies for the
RT binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-
RT 5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to human isoform
RT II.";
RL Bioorg. Med. Chem. Lett. 16:6204-6208(2006).
RN [75]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L- AND D-HISTIDINE,
RP AND ACTIVITY REGULATION.
RX PubMed=16807956; DOI=10.1002/chem.200600159;
RA Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII,
RT and XIV with l- and d-histidine and crystallographic analysis of their
RT adducts with isoform II: engineering proton-transfer processes within the
RT active site of an enzyme.";
RL Chemistry 12:7057-7066(2006).
RN [76]
RP X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH TWO-PRONG
RP INHIBITORS.
RX PubMed=16506782; DOI=10.1021/ja057257n;
RA Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S.,
RA Srivastava D.K., Christianson D.W.;
RT "Ultrahigh resolution crystal structures of human carbonic anhydrases I and
RT II complexed with 'two-prong' inhibitors reveal the molecular basis of high
RT affinity.";
RL J. Am. Chem. Soc. 128:3011-3018(2006).
RN [77]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX PubMed=16787097; DOI=10.1021/ja061574s;
RA Alterio V., Vitale R.M., Monti S.M., Pedone C., Scozzafava A., Cecchi A.,
RA De Simone G., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: X-ray and molecular modeling study for the
RT interaction of a fluorescent antitumor sulfonamide with isozyme II and
RT IX.";
RL J. Am. Chem. Soc. 128:8329-8335(2006).
RN [78]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH L- AND
RP D-PHENYLALANINE, AND ACTIVITY REGULATION.
RX PubMed=16686544; DOI=10.1021/jm0603320;
RA Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII,
RT and XIV with L- and D-phenylalanine and crystallographic analysis of their
RT adducts with isozyme II: stereospecific recognition within the active site
RT of an enzyme and its consequences for the drug design.";
RL J. Med. Chem. 49:3019-3027(2006).
RN [79]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX PubMed=16942027; DOI=10.1021/jm060531j;
RA De Simone G., Vitale R.M., Di Fiore A., Pedone C., Scozzafava A.,
RA Montero J.-L., Winum J.-Y., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides
RT incorporating disulfide bonds that target the tumor-associated isoform
RT IX.";
RL J. Med. Chem. 49:5544-5551(2006).
RN [80]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX PubMed=17125255; DOI=10.1021/jm060807n;
RA Winum J.Y., Temperini C., El Cheikh K., Innocenti A., Vullo D.,
RA Ciattini S., Montero J.-L., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: clash with Ala65 as a means for designing
RT inhibitors with low affinity for the ubiquitous isozyme II, exemplified by
RT the crystal structure of the topiramate sulfamide analogue.";
RL J. Med. Chem. 49:7024-7031(2006).
RN [81]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=17181151; DOI=10.1021/jm060705x;
RA Leese M.P., Leblond B., Smith A., Newman S.P., Di Fiore A., De Simone G.,
RA Supuran C.T., Purohit A., Reed M.J., Potter B.V.;
RT "2-substituted estradiol bis-sulfamates, multitargeted antitumor agents:
RT synthesis, in vitro SAR, protein crystallography, and in vivo activity.";
RL J. Med. Chem. 49:7683-7696(2006).
RN [82]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SACCHARIN, AND
RP ACTIVITY REGULATION.
RX PubMed=17705204; DOI=10.1002/anie.200701189;
RA Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A.,
RA Supuran C.T., Klebe G.;
RT "Saccharin inhibits carbonic anhydrases: possible explanation for its
RT unpleasant metallic aftertaste.";
RL Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
RN [83]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RX PubMed=17319692; DOI=10.1021/bi062066y;
RA Fisher S.Z., Maupin C.M., Budayova-Spano M., Govindasamy L., Tu C.,
RA Agbandje-McKenna M., Silverman D.N., Voth G.A., McKenna R.;
RT "Atomic crystal and molecular dynamics simulation structures of human
RT carbonic anhydrase II: insights into the proton transfer mechanism.";
RL Biochemistry 46:2930-2937(2007).
RN [84]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), MUTAGENESIS OF TYR-7; ASN-62 AND
RP ASN-67, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17330962; DOI=10.1021/bi602620k;
RA Fisher S.Z., Tu C., Bhatt D., Govindasamy L., Agbandje-McKenna M.,
RA McKenna R., Silverman D.N.;
RT "Speeding up proton transfer in a fast enzyme: kinetic and crystallographic
RT studies on the effect of hydrophobic amino acid substitutions in the active
RT site of human carbonic anhydrase II.";
RL Biochemistry 46:3803-3813(2007).
RN [85]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACTIVATOR
RP L-ADRENALINE, AND ACTIVITY REGULATION.
RX PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027;
RA Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.;
RT "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance
RT of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.";
RL Bioorg. Med. Chem. Lett. 17:628-635(2007).
RN [86]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITOR, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=17251017; DOI=10.1016/j.bmcl.2006.12.099;
RA Di Fiore A., Scozzafava A., Winum J.-Y., Montero J.-L., Pedone C.,
RA Supuran C.T., De Simone G.;
RT "Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-
RT sulfanilamide derivative to human isoform II and its consequences for the
RT drug design of enzyme inhibitors incorporating sugar moieties.";
RL Bioorg. Med. Chem. Lett. 17:1726-1731(2007).
RN [87]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP N-HYDROXYSULFAMIDE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17346964; DOI=10.1016/j.bmcl.2007.02.068;
RA Temperini C., Winum J.Y., Montero J.L., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: the X-ray crystal structure of the adduct
RT of N-hydroxysulfamide with isozyme II explains why this new zinc binding
RT function is effective in the design of potent inhibitors.";
RL Bioorg. Med. Chem. Lett. 17:2795-2801(2007).
RN [88]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=17540563; DOI=10.1016/j.bmcl.2007.05.045;
RA Alterio V., De Simone G., Monti S.M., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: inhibition of human, bacterial, and
RT archaeal isozymes with benzene-1,3-disulfonamides -- solution and
RT crystallographic studies.";
RL Bioorg. Med. Chem. Lett. 17:4201-4207(2007).
RN [89]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=17588751; DOI=10.1016/j.bmcl.2007.06.044;
RA Temperini C., Innocenti A., Mastrolorenzo A., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug
RT sulthiame with twelve mammalian isoforms: kinetic and X-ray
RT crystallographic studies.";
RL Bioorg. Med. Chem. Lett. 17:4866-4872(2007).
RN [90]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 4-METHYLIMIDAZOLE,
RP AND MUTAGENESIS OF TRP-5 AND HIS-64.
RX PubMed=17071654; DOI=10.1529/biophysj.106.093203;
RA Bhatt D., Fisher S.Z., Tu C., McKenna R., Silverman D.N.;
RT "Location of binding sites in small molecule rescue of human carbonic
RT anhydrase II.";
RL Biophys. J. 92:562-570(2007).
RN [91]
RP X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=17407288; DOI=10.1021/ja068359w;
RA Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S.,
RA Kooren J., Mallik S., Christianson D.W.;
RT "Structural analysis of charge discrimination in the binding of inhibitors
RT to human carbonic anhydrases I and II.";
RL J. Am. Chem. Soc. 129:5528-5537(2007).
RN [92]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP THIOXOLONE, AND ACTIVITY REGULATION.
RX PubMed=18266323; DOI=10.1021/bi702385k;
RA Barrese A.A. III, Genis C., Fisher S.Z., Orwenyo J.N., Kumara M.T.,
RA Dutta S.K., Phillips E., Kiddle J.J., Tu C., Silverman D.N.,
RA Govindasamy L., Agbandje-McKenna M., McKenna R., Tripp B.C.;
RT "Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and
RT structural study.";
RL Biochemistry 47:3174-3184(2008).
RN [93]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANTS, MUTAGENESIS OF ASN-62,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18942852; DOI=10.1021/bi801473w;
RA Zheng J., Avvaru B.S., Tu C., McKenna R., Silverman D.N.;
RT "Role of hydrophilic residues in proton transfer during catalysis by human
RT carbonic anhydrase II.";
RL Biochemistry 47:12028-12036(2008).
RN [94]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=18024029; DOI=10.1016/j.bmcl.2007.10.110;
RA Guezel O., Temperini C., Innocenti A., Scozzafava A., Salman A.,
RA Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-
RT phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-
RT ray crystallographic studies.";
RL Bioorg. Med. Chem. Lett. 18:152-158(2008).
RN [95]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=18162396; DOI=10.1016/j.bmcl.2007.12.022;
RA Temperini C., Cecchi A., Boyle N.A., Scozzafava A., Cabeza J.E.,
RA Wentworth P. Jr., Blackburn G.M., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-
RT thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-
RT ray crystallographic studies.";
RL Bioorg. Med. Chem. Lett. 18:999-1005(2008).
RN [96]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=18374572; DOI=10.1016/j.bmcl.2008.03.051;
RA Temperini C., Cecchi A., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Interaction of indapamide and related
RT diuretics with 12 mammalian isozymes and X-ray crystallographic studies for
RT the indapamide-isozyme II adduct.";
RL Bioorg. Med. Chem. Lett. 18:2567-2573(2008).
RN [97]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=18359629; DOI=10.1016/j.bmcl.2008.03.023;
RA Di Fiore A., Pedone C., Antel J., Waldeck H., Witte A., Wurl M.,
RA Scozzafava A., Supuran C.T., De Simone G.;
RT "Carbonic anhydrase inhibitors: the X-ray crystal structure of
RT ethoxzolamide complexed to human isoform II reveals the importance of
RT thr200 and gln92 for obtaining tight-binding inhibitors.";
RL Bioorg. Med. Chem. Lett. 18:2669-2674(2008).
RN [98]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=18640037; DOI=10.1016/j.bmcl.2008.06.105;
RA Temperini C., Innocenti A., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD
RT 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray
RT crystallographic studies.";
RL Bioorg. Med. Chem. Lett. 18:4282-4286(2008).
RN [99]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITORS
RP INDANESULFONAMIDES.
RX PubMed=18161740; DOI=10.1002/cmdc.200700274;
RA D'Ambrosio K., Masereel B., Thiry A., Scozzafava A., Supuran C.T.,
RA De Simone G.;
RT "Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human
RT isoform II.";
RL ChemMedChem 3:473-477(2008).
RN [100]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH (129)XE-CRYPTOPHANE
RP BIOSENSOR.
RX PubMed=18461940; DOI=10.1021/ja802214x;
RA Aaron J.A., Chambers J.M., Jude K.M., Di Costanzo L., Dmochowski I.J.,
RA Christianson D.W.;
RT "Structure of a (129)Xe-cryptophane biosensor complexed with human carbonic
RT anhydrase II.";
RL J. Am. Chem. Soc. 130:6942-6943(2008).
RN [101]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH CO2.
RX PubMed=18768466; DOI=10.1074/jbc.m805353200;
RA Domsic J.F., Avvaru B.S., Kim C.U., Gruner S.M., Agbandje-McKenna M.,
RA Silverman D.N., McKenna R.;
RT "Entrapment of carbon dioxide in the active site of carbonic anhydrase
RT II.";
RL J. Biol. Chem. 283:30766-30771(2008).
RN [102]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=18260615; DOI=10.1021/jm701319c;
RA Leese M.P., Jourdan F.L., Gaukroger K., Mahon M.F., Newman S.P.,
RA Foster P.A., Stengel C., Regis-Lydi S., Ferrandis E., Di Fiore A.,
RA De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.;
RT "Structure-activity relationships of C-17 cyano-substituted estratrienes as
RT anticancer agents.";
RL J. Med. Chem. 51:1295-1308(2008).
RN [103]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP ACTIVITY REGULATION.
RX PubMed=18481843; DOI=10.1021/jm800121c;
RA D'Ambrosio K., Vitale R.-M., Dogne J.-M., Masereel B., Innocenti A.,
RA Scozzafava A., De Simone G., Supuran C.T.;
RT "Carbonic anhydrase inhibitors: bioreductive nitro-containing sulfonamides
RT with selectivity for targeting the tumor associated isoforms IX and XII.";
RL J. Med. Chem. 51:3230-3237(2008).
RN [104]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=18723489; DOI=10.1158/1535-7163.mct-08-0195;
RA Woo L.W.L., Fischer D.S., Sharland C.M., Trusselle M., Foster P.A.,
RA Chander S.K., Di Fiore A., Supuran C.T., De Simone G., Purohit A.,
RA Reed M.J., Potter B.V.L.;
RT "Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated
RT second-generation agent, in vitro and in vivo activities, molecular
RT modeling, and protein crystallography.";
RL Mol. Cancer Ther. 7:2435-2444(2008).
RN [105]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF ALA-65 AND ASN-67.
RX PubMed=19170619; DOI=10.1021/bi802035f;
RA Genis C., Sippel K.H., Case N., Cao W., Avvaru B.S., Tartaglia L.J.,
RA Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N., Rosser C.J.,
RA McKenna R.;
RT "Design of a carbonic anhydrase IX active-site mimic to screen inhibitors
RT for possible anticancer properties.";
RL Biochemistry 48:1322-1331(2009).
RN [106]
RP X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) FREE AND IN COMPLEX WITH ZINC ION,
RP AND COFACTOR.
RX PubMed=19583303; DOI=10.1021/bi9007512;
RA Avvaru B.S., Busby S.A., Chalmers M.J., Griffin P.R., Venkatakrishnan B.,
RA Agbandje-McKenna M., Silverman D.N., McKenna R.;
RT "Apo-human carbonic anhydrase II revisited: implications of the loss of a
RT metal in protein structure, stability, and solvent network.";
RL Biochemistry 48:7365-7372(2009).
RN [107]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITOR
RP THIABENDAZOLE-5-SULFONAMIDE, AND ACTIVITY REGULATION.
RX PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA Muehlschlegel F.A., Supuran C.T.;
RT "A thiabendazole sulfonamide shows potent inhibitory activity against
RT mammalian and nematode alpha-carbonic anhydrases.";
RL Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN [108]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-260 IN COMPLEX WITH COUMARIN
RP INHIBITORS, AND ACTIVITY REGULATION.
RX PubMed=19206230; DOI=10.1021/ja809683v;
RA Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA Quinn R.J., Supuran C.T.;
RT "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT class of suicide inhibitors.";
RL J. Am. Chem. Soc. 131:3057-3062(2009).
RN [109]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=19115843; DOI=10.1021/jm801386n;
RA Temperini C., Cecchi A., Scozzafava A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Comparison of chlorthalidone and indapamide
RT X-ray crystal structures in adducts with isozyme II: when three water
RT molecules and the keto-enol tautomerism make the difference.";
RL J. Med. Chem. 52:322-328(2009).
RN [110]
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=19731956; DOI=10.1021/jm900641r;
RA Vitale R.M., Alterio V., Innocenti A., Winum J.-Y., Monti S.M.,
RA De Simone G., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-
RT sulfamate adducts with isozymes II and IX as a platform for designing
RT tight-binding, more isoform-selective inhibitors.";
RL J. Med. Chem. 52:5990-5998(2009).
RN [111]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS.
RX PubMed=19827837; DOI=10.1021/jm900914e;
RA Lopez M., Paul B., Hofmann A., Morizzi J., Wu Q.K., Charman S.A.,
RA Innocenti A., Vullo D., Supuran C.T., Poulsen S.-A.;
RT "S-glycosyl primary sulfonamides--a new structural class for selective
RT inhibition of cancer-associated carbonic anhydrases.";
RL J. Med. Chem. 52:6421-6432(2009).
RN [112]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS,
RP AND ACTIVITY REGULATION.
RX PubMed=19778001; DOI=10.1021/jp906593c;
RA Ciani L., Cecchi A., Temperini C., Supuran C.T., Ristori S.;
RT "Dissecting the inhibition mechanism of cytosolic versus transmembrane
RT carbonic anhydrases by ESR.";
RL J. Phys. Chem. B 113:13998-14005(2009).
RN [113]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND
RP ACTIVITY REGULATION.
RX PubMed=19520834; DOI=10.1073/pnas.0904184106;
RA Sjoeblom B., Polentarutti M., Djinovic-Carugo K.;
RT "Structural study of X-ray induced activation of carbonic anhydrase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10609-10613(2009).
RN [114]
RP VARIANT JOGJAKARTA GLU-18.
RX PubMed=6817747; DOI=10.1007/bf00484072;
RA Jones G.L., Sofro A.S.M., Shaw D.C.;
RT "Chemical and enzymological characterization of an Indonesian variant of
RT human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to
RT Glu).";
RL Biochem. Genet. 20:979-1000(1982).
RN [115]
RP VARIANT MELBOURNE HIS-236.
RX PubMed=6407977; DOI=10.1007/bf00274768;
RA Jones G.L., Shaw D.C.;
RT "A chemical and enzymological comparison of the common major human
RT erythrocyte carbonic anhydrase II, its minor component, and a new genetic
RT variant, CA II Melbourne (237 Pro leads to His).";
RL Hum. Genet. 63:392-399(1983).
RN [116]
RP VARIANT OPTB3 TYR-107.
RX PubMed=1928091;
RA Venta P.J., Welty R.J., Johnson T.M., Sly W.S., Tashian R.E.;
RT "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by
RT a point mutation at an invariant histidine residue (107 His-->Tyr):
RT complete structure of the normal human CA II gene.";
RL Am. J. Hum. Genet. 49:1082-1090(1991).
RN [117]
RP VARIANT OPTB3 TYR-107.
RX PubMed=1542674; DOI=10.1073/pnas.89.5.1804;
RA Roth D.E., Venta P.J., Tashian R.E., Sly W.S.;
RT "Molecular basis of human carbonic anhydrase II deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992).
RN [118]
RP VARIANT OPTB3 TYR-107.
RX PubMed=8834238; DOI=10.1007/bf02267062;
RA Soda H., Yukizane S., Yoshida I., Koga Y., Aramaki S., Kato H.;
RT "A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese
RT patients with carbonic anhydrase II deficiency with central nervous system
RT involvement.";
RL Hum. Genet. 97:435-437(1996).
RN [119]
RP VARIANT OPTB3 PRO-92.
RX PubMed=9143915;
RX DOI=10.1002/(sici)1098-1004(1997)9:5<383::aid-humu1>3.0.co;2-5;
RA Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S.;
RT "Seven novel mutations in carbonic anhydrase II deficiency syndrome
RT identified by SSCP and direct sequencing analysis.";
RL Hum. Mutat. 9:383-387(1997).
RN [120]
RP VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, FUNCTION, CATALYTIC
RP ACTIVITY, AND CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.
RX PubMed=15300855; DOI=10.1002/humu.9266;
RA Shah G.N., Bonapace G., Hu P.Y., Strisciuglio P., Sly W.S.;
RT "Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal
RT tubular acidosis and brain calcification): novel mutations in CA2
RT identified by direct sequencing expand the opportunity for genotype-
RT phenotype correlation.";
RL Hum. Mutat. 24:272-272(2004).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide
CC (PubMed:1909891, PubMed:1910042, PubMed:1336460, PubMed:8485129,
CC PubMed:8399159, PubMed:8218160, PubMed:8262987, PubMed:8451242,
CC PubMed:7901850, PubMed:7761440, PubMed:8639494, PubMed:9265618,
CC PubMed:17330962, PubMed:9398308, PubMed:11327835, PubMed:12056894,
CC PubMed:17346964, PubMed:12171926, PubMed:15453828, PubMed:16214338,
CC PubMed:15865431, PubMed:16106378, PubMed:15300855, PubMed:15667203,
CC PubMed:18942852, PubMed:11831900, PubMed:17251017). Can also hydrate
CC cyanamide to urea (PubMed:10550681, PubMed:11015219). Stimulates the
CC chloride-bicarbonate exchange activity of SLC26A6 (PubMed:15990874).
CC Essential for bone resorption and osteoclast differentiation
CC (PubMed:15300855). Involved in the regulation of fluid secretion into
CC the anterior chamber of the eye. Contributes to intracellular pH
CC regulation in the duodenal upper villous epithelium during proton-
CC coupled peptide absorption. {ECO:0000269|PubMed:10550681,
CC ECO:0000269|PubMed:11015219, ECO:0000269|PubMed:11327835,
CC ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:12056894,
CC ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:1336460,
CC ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:15453828,
CC ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:15865431,
CC ECO:0000269|PubMed:15990874, ECO:0000269|PubMed:16106378,
CC ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:17251017,
CC ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:17346964,
CC ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:1909891,
CC ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:7761440,
CC ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
CC ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159,
CC ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8485129,
CC ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:9265618,
CC ECO:0000269|PubMed:9398308}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:11327835,
CC ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:12171926,
CC ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:15453828,
CC ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:15865431,
CC ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:16214338,
CC ECO:0000269|PubMed:17251017, ECO:0000269|PubMed:17330962,
CC ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:18942852,
CC ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042,
CC ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
CC ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987,
CC ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8451242,
CC ECO:0000269|PubMed:8485129, ECO:0000269|PubMed:8639494,
CC ECO:0000269|PubMed:9265618, ECO:0000269|PubMed:9398308};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69;
CC Evidence={ECO:0000269|PubMed:10550681};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545,
CC ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293,
CC ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303,
CC ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020,
CC ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386,
CC ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
CC ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673,
CC ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430,
CC ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389,
CC ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974,
CC ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:19583303};
CC Note=Zinc. Can also use cobalt(II) with lower efficiency, but not
CC copper(II), nickel(II) and manganese(II).
CC {ECO:0000269|PubMed:19583303};
CC -!- ACTIVITY REGULATION: Activated by X-ray, histamine, L-adrenaline,
CC L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His
CC (carnosine). Competitively inhibited by saccharin, thioxolone,
CC coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-
CC 125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide
CC derivatives such as acetazolamide (AZA), methazolamide (MZA),
CC ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide,
CC dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide
CC and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and
CC Foscarnet (phosphonoformate trisodium salt). Repressed strongly by
CC hydrogen sulfide(HS) and weakly by nitrate (NO(3)). Esterase activity
CC weakly reduced by cyanamide. N-hydroxyurea interfers with zinc binding
CC and inhibit activity. {ECO:0000269|PubMed:11802772,
CC ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236,
CC ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146,
CC ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856,
CC ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057,
CC ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17540563,
CC ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204,
CC ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396,
CC ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572,
CC ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18618712,
CC ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:1910042,
CC ECO:0000269|PubMed:19170619, ECO:0000269|PubMed:19186056,
CC ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19520834,
CC ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:9265618}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.3 mM for CO(2) {ECO:0000269|PubMed:18618712,
CC ECO:0000269|PubMed:7761440};
CC KM=11 mM for CO(2) {ECO:0000269|PubMed:1909891};
CC KM=8.2 mM for CO(2) {ECO:0000269|PubMed:9398308};
CC KM=82 mM for H(2)CO(3) {ECO:0000269|PubMed:8262987};
CC KM=2.9 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681};
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:15667203,
CC ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852,
CC ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:9398308};
CC -!- SUBUNIT: Interacts with SLC4A4 (PubMed:14567693, PubMed:15218065).
CC Interaction with SLC4A7 regulates SLC4A7 transporter activity
CC (PubMed:14736710). Interacts with SLC26A6 isoform 4 (via C-terminus
CC cytoplasmic domain) (PubMed:15990874). {ECO:0000269|PubMed:14567693,
CC ECO:0000269|PubMed:14736710, ECO:0000269|PubMed:15218065,
CC ECO:0000269|PubMed:15990874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15990874}. Cell
CC membrane {ECO:0000269|PubMed:15990874}. Note=Colocalized with SLC26A6
CC at the surface of the cell membrane in order to form a bicarbonate
CC transport metabolon. Displaced from the cytosolic surface of the cell
CC membrane by PKC in phorbol myristate acetate (PMA)-induced cells.
CC {ECO:0000269|PubMed:15990874}.
CC -!- DISEASE: Osteopetrosis, autosomal recessive 3 (OPTB3) [MIM:259730]: A
CC rare genetic disease characterized by abnormally dense bone, due to
CC defective resorption of immature bone. Osteopetrosis occurs in two
CC forms: a severe autosomal recessive form occurring in utero, infancy,
CC or childhood, and a benign autosomal dominant form occurring in
CC adolescence or adulthood. Recessive osteopetrosis commonly manifests in
CC early infancy with macrocephaly, feeding difficulties, evolving
CC blindness and deafness, bone marrow failure, severe anemia, and
CC hepatosplenomegaly. Deafness and blindness are generally thought to
CC represent effects of pressure on nerves. OPTB3 is associated with renal
CC tubular acidosis, cerebral calcification (marble brain disease) and in
CC some cases with intellectual disability. {ECO:0000269|PubMed:15300855,
CC ECO:0000269|PubMed:1542674, ECO:0000269|PubMed:1928091,
CC ECO:0000269|PubMed:8834238, ECO:0000269|PubMed:9143915}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Target of drugs used in treatments against glaucoma
CC disorder and breast cancer. {ECO:0000269|PubMed:17251017}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M77181; AAA51909.1; -; Genomic_DNA.
DR EMBL; M77176; AAA51909.1; JOINED; Genomic_DNA.
DR EMBL; M77177; AAA51909.1; JOINED; Genomic_DNA.
DR EMBL; M77178; AAA51909.1; JOINED; Genomic_DNA.
DR EMBL; M77179; AAA51909.1; JOINED; Genomic_DNA.
DR EMBL; M77180; AAA51909.1; JOINED; Genomic_DNA.
DR EMBL; Y00339; CAA68426.1; -; mRNA.
DR EMBL; X03251; CAA27012.1; -; Genomic_DNA.
DR EMBL; J03037; AAA51908.1; -; mRNA.
DR EMBL; CR536526; CAG38763.1; -; mRNA.
DR EMBL; CR541875; CAG46673.1; -; mRNA.
DR EMBL; AK312978; BAG35815.1; -; mRNA.
DR EMBL; CH471068; EAW87136.1; -; Genomic_DNA.
DR EMBL; BC011949; AAH11949.1; -; mRNA.
DR EMBL; M36532; AAA51911.1; -; mRNA.
DR CCDS; CCDS6239.1; -.
DR PIR; A27175; CRHU2.
DR RefSeq; NP_000058.1; NM_000067.2.
DR PDB; 12CA; X-ray; 2.40 A; A=1-260.
DR PDB; 1A42; X-ray; 2.25 A; A=2-260.
DR PDB; 1AM6; X-ray; 2.00 A; A=2-260.
DR PDB; 1AVN; X-ray; 2.00 A; A=2-260.
DR PDB; 1BCD; X-ray; 1.90 A; A=2-260.
DR PDB; 1BIC; X-ray; 1.90 A; A=2-260.
DR PDB; 1BN1; X-ray; 2.10 A; A=2-260.
DR PDB; 1BN3; X-ray; 2.20 A; A=2-260.
DR PDB; 1BN4; X-ray; 2.10 A; A=2-260.
DR PDB; 1BNM; X-ray; 2.60 A; A=2-260.
DR PDB; 1BNN; X-ray; 2.30 A; A=2-260.
DR PDB; 1BNQ; X-ray; 2.40 A; A=2-260.
DR PDB; 1BNT; X-ray; 2.15 A; A=2-260.
DR PDB; 1BNU; X-ray; 2.15 A; A=2-260.
DR PDB; 1BNV; X-ray; 2.40 A; A=2-260.
DR PDB; 1BNW; X-ray; 2.25 A; A=2-260.
DR PDB; 1BV3; X-ray; 1.85 A; A=2-260.
DR PDB; 1CA2; X-ray; 2.00 A; A=2-260.
DR PDB; 1CA3; X-ray; 2.30 A; A=1-260.
DR PDB; 1CAH; X-ray; 1.88 A; A=2-260.
DR PDB; 1CAI; X-ray; 1.80 A; A=2-260.
DR PDB; 1CAJ; X-ray; 1.90 A; A=2-260.
DR PDB; 1CAK; X-ray; 1.90 A; A=2-260.
DR PDB; 1CAL; X-ray; 2.20 A; A=2-260.
DR PDB; 1CAM; X-ray; 1.70 A; A=2-260.
DR PDB; 1CAN; X-ray; 1.90 A; A=2-260.
DR PDB; 1CAO; X-ray; 1.90 A; A=2-260.
DR PDB; 1CAY; X-ray; 2.10 A; A=2-260.
DR PDB; 1CAZ; X-ray; 1.90 A; A=2-260.
DR PDB; 1CCS; X-ray; 2.35 A; A=2-260.
DR PDB; 1CCT; X-ray; 2.20 A; A=2-260.
DR PDB; 1CCU; X-ray; 2.25 A; A=2-260.
DR PDB; 1CIL; X-ray; 1.60 A; A=2-260.
DR PDB; 1CIM; X-ray; 2.10 A; A=2-260.
DR PDB; 1CIN; X-ray; 2.10 A; A=2-260.
DR PDB; 1CNB; X-ray; 2.35 A; A=2-260.
DR PDB; 1CNC; X-ray; 2.20 A; A=2-260.
DR PDB; 1CNG; X-ray; 1.90 A; A=2-260.
DR PDB; 1CNH; X-ray; 2.05 A; A=2-260.
DR PDB; 1CNI; X-ray; 1.80 A; A=2-260.
DR PDB; 1CNJ; X-ray; 1.80 A; A=2-260.
DR PDB; 1CNK; X-ray; 2.15 A; A=2-260.
DR PDB; 1CNW; X-ray; 2.00 A; A=1-260.
DR PDB; 1CNX; X-ray; 1.90 A; A=1-260.
DR PDB; 1CNY; X-ray; 2.30 A; A=1-260.
DR PDB; 1CRA; X-ray; 1.90 A; A=2-260.
DR PDB; 1CVA; X-ray; 2.25 A; A=2-260.
DR PDB; 1CVB; X-ray; 2.40 A; A=2-260.
DR PDB; 1CVC; X-ray; 2.30 A; A=2-260.
DR PDB; 1CVD; X-ray; 2.20 A; A=5-259.
DR PDB; 1CVE; X-ray; 2.25 A; A=2-260.
DR PDB; 1CVF; X-ray; 2.25 A; A=2-260.
DR PDB; 1CVH; X-ray; 2.30 A; A=5-259.
DR PDB; 1DCA; X-ray; 2.20 A; A=1-260.
DR PDB; 1DCB; X-ray; 2.10 A; A=1-260.
DR PDB; 1EOU; X-ray; 2.10 A; A=1-260.
DR PDB; 1F2W; X-ray; 1.90 A; A=2-260.
DR PDB; 1FQL; X-ray; 2.00 A; A=1-260.
DR PDB; 1FQM; X-ray; 2.00 A; A=1-260.
DR PDB; 1FQN; X-ray; 2.00 A; A=1-260.
DR PDB; 1FQR; X-ray; 2.00 A; A=1-260.
DR PDB; 1FR4; X-ray; 1.60 A; A=1-260.
DR PDB; 1FR7; X-ray; 1.50 A; A/B=1-260.
DR PDB; 1FSN; X-ray; 2.00 A; A/B=1-260.
DR PDB; 1FSQ; X-ray; 2.00 A; A/B=1-260.
DR PDB; 1FSR; X-ray; 2.00 A; A/B=1-260.
DR PDB; 1G0E; X-ray; 1.60 A; A=1-260.
DR PDB; 1G0F; X-ray; 1.60 A; A=1-260.
DR PDB; 1G1D; X-ray; 2.04 A; A=2-260.
DR PDB; 1G3Z; X-ray; 1.86 A; A=2-260.
DR PDB; 1G45; X-ray; 1.83 A; A=2-260.
DR PDB; 1G46; X-ray; 1.84 A; A=2-260.
DR PDB; 1G48; X-ray; 1.86 A; A=2-260.
DR PDB; 1G4J; X-ray; 1.84 A; A=2-260.
DR PDB; 1G4O; X-ray; 1.96 A; A=2-260.
DR PDB; 1G52; X-ray; 1.80 A; A=2-260.
DR PDB; 1G53; X-ray; 1.94 A; A=2-260.
DR PDB; 1G54; X-ray; 1.86 A; A=2-260.
DR PDB; 1H4N; X-ray; 2.00 A; A=2-260.
DR PDB; 1H9N; X-ray; 1.85 A; A=2-260.
DR PDB; 1H9Q; X-ray; 2.20 A; A=2-260.
DR PDB; 1HCA; X-ray; 2.30 A; A=1-260.
DR PDB; 1HEA; X-ray; 2.00 A; A=1-260.
DR PDB; 1HEB; X-ray; 2.00 A; A=1-260.
DR PDB; 1HEC; X-ray; 2.00 A; A=1-260.
DR PDB; 1HED; X-ray; 2.00 A; A=1-260.
DR PDB; 1HVA; X-ray; 2.30 A; A=1-260.
DR PDB; 1I8Z; X-ray; 1.93 A; A=2-260.
DR PDB; 1I90; X-ray; 2.00 A; A=2-260.
DR PDB; 1I91; X-ray; 2.00 A; A=2-260.
DR PDB; 1I9L; X-ray; 1.93 A; A=2-260.
DR PDB; 1I9M; X-ray; 1.84 A; A=2-260.
DR PDB; 1I9N; X-ray; 1.86 A; A=2-260.
DR PDB; 1I9O; X-ray; 1.86 A; A=2-260.
DR PDB; 1I9P; X-ray; 1.92 A; A=2-260.
DR PDB; 1I9Q; X-ray; 1.80 A; A=2-260.
DR PDB; 1IF4; X-ray; 1.93 A; A=2-260.
DR PDB; 1IF5; X-ray; 2.00 A; A=2-260.
DR PDB; 1IF6; X-ray; 2.09 A; A=2-259.
DR PDB; 1IF7; X-ray; 1.98 A; A=2-260.
DR PDB; 1IF8; X-ray; 1.94 A; A=2-260.
DR PDB; 1IF9; X-ray; 2.00 A; A=2-260.
DR PDB; 1KWQ; X-ray; 2.60 A; A=1-260.
DR PDB; 1KWR; X-ray; 2.25 A; A=1-260.
DR PDB; 1LG5; X-ray; 1.75 A; A=1-260.
DR PDB; 1LG6; X-ray; 2.20 A; A=1-260.
DR PDB; 1LGD; X-ray; 1.90 A; A=1-260.
DR PDB; 1LUG; X-ray; 0.95 A; A=2-260.
DR PDB; 1LZV; X-ray; 2.30 A; A=1-260.
DR PDB; 1MOO; X-ray; 1.05 A; A=1-260.
DR PDB; 1MUA; X-ray; 1.70 A; A=4-259.
DR PDB; 1OKL; X-ray; 2.10 A; A=2-260.
DR PDB; 1OKM; X-ray; 2.20 A; A=2-260.
DR PDB; 1OKN; X-ray; 2.40 A; A=2-260.
DR PDB; 1OQ5; X-ray; 1.50 A; A=2-259.
DR PDB; 1RAY; X-ray; 1.80 A; A=2-260.
DR PDB; 1RAZ; X-ray; 1.90 A; A=2-260.
DR PDB; 1RZA; X-ray; 1.90 A; A=2-260.
DR PDB; 1RZB; X-ray; 1.80 A; A=2-260.
DR PDB; 1RZC; X-ray; 1.90 A; A=2-260.
DR PDB; 1RZD; X-ray; 1.90 A; A=2-260.
DR PDB; 1RZE; X-ray; 1.90 A; A=2-260.
DR PDB; 1T9N; X-ray; 2.00 A; A=1-259.
DR PDB; 1TB0; X-ray; 2.00 A; X=1-259.
DR PDB; 1TBT; X-ray; 2.00 A; X=1-259.
DR PDB; 1TE3; X-ray; 2.00 A; X=1-260.
DR PDB; 1TEQ; X-ray; 2.00 A; X=1-260.
DR PDB; 1TEU; X-ray; 2.00 A; X=1-260.
DR PDB; 1TG3; X-ray; 1.80 A; A=1-260.
DR PDB; 1TG9; X-ray; 1.90 A; A=1-260.
DR PDB; 1TH9; X-ray; 1.63 A; A=1-260.
DR PDB; 1THK; X-ray; 1.80 A; A=1-260.
DR PDB; 1TTM; X-ray; 1.95 A; A=2-259.
DR PDB; 1UGA; X-ray; 2.00 A; A=3-260.
DR PDB; 1UGB; X-ray; 2.00 A; A=3-260.
DR PDB; 1UGC; X-ray; 2.00 A; A=3-260.
DR PDB; 1UGD; X-ray; 2.00 A; A=3-260.
DR PDB; 1UGE; X-ray; 1.90 A; A=3-260.
DR PDB; 1UGF; X-ray; 2.00 A; A=3-260.
DR PDB; 1UGG; X-ray; 2.20 A; A=3-260.
DR PDB; 1XEG; X-ray; 1.81 A; A=1-260.
DR PDB; 1XEV; X-ray; 2.20 A; A/B/C/D=1-260.
DR PDB; 1XPZ; X-ray; 2.02 A; A=3-260.
DR PDB; 1XQ0; X-ray; 1.76 A; A=2-260.
DR PDB; 1YDA; X-ray; 2.10 A; A=2-260.
DR PDB; 1YDB; X-ray; 1.90 A; A=2-260.
DR PDB; 1YDC; X-ray; 1.95 A; A=2-260.
DR PDB; 1YDD; X-ray; 2.10 A; A=2-260.
DR PDB; 1YO0; X-ray; 1.80 A; A=1-260.
DR PDB; 1YO1; X-ray; 1.70 A; A=1-260.
DR PDB; 1YO2; X-ray; 1.80 A; A=1-259.
DR PDB; 1Z9Y; X-ray; 1.66 A; A=2-259.
DR PDB; 1ZE8; X-ray; 2.00 A; A=2-260.
DR PDB; 1ZFK; X-ray; 1.56 A; A=2-259.
DR PDB; 1ZFQ; X-ray; 1.55 A; A=2-259.
DR PDB; 1ZGE; X-ray; 1.65 A; A=2-259.
DR PDB; 1ZGF; X-ray; 1.75 A; A=2-259.
DR PDB; 1ZH9; X-ray; 1.70 A; A=2-259.
DR PDB; 1ZSA; X-ray; 2.50 A; A=2-260.
DR PDB; 1ZSB; X-ray; 2.00 A; A=2-260.
DR PDB; 1ZSC; X-ray; 1.80 A; A=2-260.
DR PDB; 2ABE; X-ray; 2.00 A; A=2-259.
DR PDB; 2AW1; X-ray; 1.46 A; A=2-260.
DR PDB; 2AX2; X-ray; 1.50 A; A=1-259.
DR PDB; 2CA2; X-ray; 1.90 A; A=2-260.
DR PDB; 2CBA; X-ray; 1.54 A; A=2-260.
DR PDB; 2CBB; X-ray; 1.67 A; A=2-260.
DR PDB; 2CBC; X-ray; 1.88 A; A=2-260.
DR PDB; 2CBD; X-ray; 1.67 A; A=2-260.
DR PDB; 2CBE; X-ray; 1.82 A; A=2-260.
DR PDB; 2EU2; X-ray; 1.15 A; A=1-260.
DR PDB; 2EU3; X-ray; 1.60 A; A=1-260.
DR PDB; 2EZ7; X-ray; 2.00 A; A=1-259.
DR PDB; 2F14; X-ray; 1.71 A; A=2-259.
DR PDB; 2FMG; X-ray; 1.60 A; A=1-259.
DR PDB; 2FMZ; X-ray; 1.60 A; A=1-259.
DR PDB; 2FNK; X-ray; 1.80 A; A=1-260.
DR PDB; 2FNM; X-ray; 1.80 A; A=1-260.
DR PDB; 2FNN; X-ray; 1.80 A; A=1-260.
DR PDB; 2FOQ; X-ray; 1.25 A; A=1-259.
DR PDB; 2FOS; X-ray; 1.10 A; A=1-259.
DR PDB; 2FOU; X-ray; 0.99 A; A=1-259.
DR PDB; 2FOV; X-ray; 1.15 A; A=1-259.
DR PDB; 2GD8; X-ray; 1.46 A; A=2-259.
DR PDB; 2GEH; X-ray; 2.00 A; A=1-259.
DR PDB; 2H15; X-ray; 1.90 A; A=1-259.
DR PDB; 2H4N; X-ray; 1.90 A; A=2-260.
DR PDB; 2HD6; X-ray; 1.80 A; A=2-259.
DR PDB; 2HKK; X-ray; 1.90 A; A=1-260.
DR PDB; 2HL4; X-ray; 1.55 A; A=2-260.
DR PDB; 2HNC; X-ray; 1.55 A; A=2-259.
DR PDB; 2HOC; X-ray; 2.10 A; A=2-259.
DR PDB; 2ILI; X-ray; 1.05 A; A=2-259.
DR PDB; 2NNG; X-ray; 1.20 A; A=2-260.
DR PDB; 2NNO; X-ray; 1.01 A; A=2-260.
DR PDB; 2NNS; X-ray; 1.03 A; A=2-260.
DR PDB; 2NNV; X-ray; 1.10 A; A=2-260.
DR PDB; 2NWO; X-ray; 1.70 A; A=1-259.
DR PDB; 2NWP; X-ray; 1.80 A; A=1-259.
DR PDB; 2NWY; X-ray; 1.65 A; A=1-259.
DR PDB; 2NWZ; X-ray; 1.80 A; A=1-259.
DR PDB; 2NXR; X-ray; 1.70 A; A=1-259.
DR PDB; 2NXS; X-ray; 1.80 A; A=1-259.
DR PDB; 2NXT; X-ray; 1.15 A; A=1-260.
DR PDB; 2O4Z; X-ray; 2.10 A; A=1-260.
DR PDB; 2OSF; X-ray; 1.60 A; A=2-260.
DR PDB; 2OSM; X-ray; 1.60 A; A=2-260.
DR PDB; 2POU; X-ray; 1.60 A; A=1-259.
DR PDB; 2POV; X-ray; 1.60 A; A=1-258.
DR PDB; 2POW; X-ray; 1.75 A; A=1-259.
DR PDB; 2Q1B; X-ray; 1.70 A; A=1-260.
DR PDB; 2Q1Q; X-ray; 1.90 A; A=1-260.
DR PDB; 2Q38; X-ray; 1.95 A; A=1-260.
DR PDB; 2QO8; X-ray; 1.40 A; A=2-260.
DR PDB; 2QOA; X-ray; 1.60 A; A=2-260.
DR PDB; 2QP6; X-ray; 1.45 A; A=2-260.
DR PDB; 2VVA; X-ray; 1.56 A; X=1-260.
DR PDB; 2VVB; X-ray; 1.66 A; X=1-260.
DR PDB; 2WD2; X-ray; 1.49 A; A=2-259.
DR PDB; 2WD3; X-ray; 1.80 A; A=2-260.
DR PDB; 2WEG; X-ray; 1.10 A; A=2-260.
DR PDB; 2WEH; X-ray; 2.09 A; A=2-260.
DR PDB; 2WEJ; X-ray; 1.45 A; A=2-260.
DR PDB; 2WEO; X-ray; 1.40 A; A=2-260.
DR PDB; 2X7S; X-ray; 1.64 A; A=2-260.
DR PDB; 2X7T; X-ray; 1.89 A; A=2-260.
DR PDB; 2X7U; X-ray; 2.12 A; A=2-260.
DR PDB; 3B4F; X-ray; 1.89 A; A=1-260.
DR PDB; 3BET; X-ray; 1.85 A; A=2-260.
DR PDB; 3BL0; X-ray; 1.90 A; A=1-260.
DR PDB; 3BL1; X-ray; 2.10 A; A=1-260.
DR PDB; 3C7P; X-ray; 1.70 A; A=1-260.
DR PDB; 3CA2; X-ray; 2.00 A; A=2-260.
DR PDB; 3CAJ; X-ray; 1.80 A; A=1-260.
DR PDB; 3CYU; X-ray; 1.70 A; A=1-260.
DR PDB; 3D8W; X-ray; 1.70 A; A=1-260.
DR PDB; 3D92; X-ray; 1.10 A; A=1-260.
DR PDB; 3D93; X-ray; 1.10 A; A=1-260.
DR PDB; 3D9Z; X-ray; 1.65 A; A=1-260.
DR PDB; 3DAZ; X-ray; 1.60 A; A=1-260.
DR PDB; 3DBU; X-ray; 1.70 A; A=1-260.
DR PDB; 3DC3; X-ray; 1.70 A; A=1-260.
DR PDB; 3DC9; X-ray; 1.60 A; A=1-260.
DR PDB; 3DCC; X-ray; 1.60 A; A=1-260.
DR PDB; 3DCS; X-ray; 1.80 A; A=1-260.
DR PDB; 3DCW; X-ray; 1.50 A; A=1-260.
DR PDB; 3DD0; X-ray; 1.48 A; A=1-260.
DR PDB; 3DD8; X-ray; 1.90 A; A=1-260.
DR PDB; 3DV7; X-ray; 1.70 A; A=2-260.
DR PDB; 3DVB; X-ray; 1.70 A; A=2-260.
DR PDB; 3DVC; X-ray; 1.60 A; A=2-260.
DR PDB; 3DVD; X-ray; 1.60 A; A=2-260.
DR PDB; 3EFI; X-ray; 1.75 A; A=2-260.
DR PDB; 3EFT; X-ray; 1.85 A; A=1-260.
DR PDB; 3F4X; X-ray; 1.90 A; A=1-260.
DR PDB; 3F8E; X-ray; 2.00 A; A=1-260.
DR PDB; 3FFP; X-ray; 1.81 A; X=1-260.
DR PDB; 3GZ0; X-ray; 1.26 A; A=2-260.
DR PDB; 3HFP; X-ray; 2.10 A; A=1-260.
DR PDB; 3HKN; X-ray; 1.80 A; A=1-260.
DR PDB; 3HKQ; X-ray; 1.70 A; A=1-260.
DR PDB; 3HKT; X-ray; 2.36 A; A=1-260.
DR PDB; 3HKU; X-ray; 1.80 A; A=1-260.
DR PDB; 3HLJ; X-ray; 1.44 A; A=1-260.
DR PDB; 3HS4; X-ray; 1.10 A; A=1-260.
DR PDB; 3IBI; X-ray; 1.93 A; A=2-260.
DR PDB; 3IBL; X-ray; 1.55 A; A=2-260.
DR PDB; 3IBN; X-ray; 2.20 A; A=2-260.
DR PDB; 3IBU; X-ray; 1.41 A; A=2-260.
DR PDB; 3IEO; X-ray; 2.00 A; A=1-260.
DR PDB; 3IGP; X-ray; 1.65 A; A=1-260.
DR PDB; 3K2F; X-ray; 1.98 A; A=1-260.
DR PDB; 3K34; X-ray; 0.90 A; A=1-260.
DR PDB; 3K7K; X-ray; 1.90 A; A=1-260.
DR PDB; 3KIG; X-ray; 1.39 A; A=1-260.
DR PDB; 3KKX; Neutron; 2.00 A; A=1-260.
DR PDB; 3KNE; X-ray; 1.35 A; A=1-260.
DR PDB; 3KOI; X-ray; 1.64 A; A=1-260.
DR PDB; 3KOK; X-ray; 1.50 A; A=1-260.
DR PDB; 3KON; X-ray; 1.50 A; A=1-260.
DR PDB; 3KS3; X-ray; 0.90 A; A=1-260.
DR PDB; 3KWA; X-ray; 2.00 A; A=1-260.
DR PDB; 3L14; X-ray; 1.22 A; A=1-260.
DR PDB; 3M04; X-ray; 1.40 A; A=1-260.
DR PDB; 3M14; X-ray; 1.38 A; A=1-260.
DR PDB; 3M1J; X-ray; 1.80 A; A=1-260.
DR PDB; 3M1K; X-ray; 1.35 A; A=1-260.
DR PDB; 3M1Q; X-ray; 1.69 A; A=1-260.
DR PDB; 3M1W; X-ray; 1.38 A; A=1-260.
DR PDB; 3M2N; X-ray; 1.65 A; A=1-260.
DR PDB; 3M2X; X-ray; 1.87 A; A=1-260.
DR PDB; 3M2Y; X-ray; 1.17 A; A=1-260.
DR PDB; 3M2Z; X-ray; 1.70 A; A=1-260.
DR PDB; 3M3X; X-ray; 1.68 A; A=1-260.
DR PDB; 3M40; X-ray; 1.60 A; A=1-260.
DR PDB; 3M5E; X-ray; 1.70 A; A=1-260.
DR PDB; 3M5S; X-ray; 1.40 A; A=1-260.
DR PDB; 3M5T; X-ray; 1.95 A; A=1-260.
DR PDB; 3M67; X-ray; 1.80 A; A=1-260.
DR PDB; 3M96; X-ray; 1.40 A; A=1-260.
DR PDB; 3M98; X-ray; 1.50 A; A=1-260.
DR PDB; 3MHC; X-ray; 1.70 A; A=1-260.
DR PDB; 3MHI; X-ray; 1.70 A; A=1-260.
DR PDB; 3MHL; X-ray; 1.90 A; A=1-260.
DR PDB; 3MHM; X-ray; 1.50 A; A=1-260.
DR PDB; 3MHO; X-ray; 1.15 A; A=1-260.
DR PDB; 3ML2; X-ray; 1.80 A; A=1-260.
DR PDB; 3MMF; X-ray; 1.50 A; A=1-260.
DR PDB; 3MNA; X-ray; 1.50 A; A=1-260.
DR PDB; 3MNH; X-ray; 1.65 A; A=1-260.
DR PDB; 3MNI; X-ray; 1.75 A; A=1-260.
DR PDB; 3MNJ; X-ray; 1.75 A; A=1-260.
DR PDB; 3MNK; X-ray; 1.75 A; A=1-260.
DR PDB; 3MNU; X-ray; 1.80 A; A=2-260.
DR PDB; 3MWO; X-ray; 1.40 A; A/B=1-260.
DR PDB; 3MYQ; X-ray; 1.35 A; A=1-260.
DR PDB; 3MZC; X-ray; 1.50 A; A=1-260.
DR PDB; 3N0N; X-ray; 1.50 A; A=1-260.
DR PDB; 3N2P; X-ray; 1.65 A; A=1-260.
DR PDB; 3N3J; X-ray; 1.50 A; A=1-260.
DR PDB; 3N4B; X-ray; 1.60 A; A=1-260.
DR PDB; 3NB5; X-ray; 1.80 A; A=1-260.
DR PDB; 3NI5; X-ray; 2.10 A; A=1-260.
DR PDB; 3NJ9; X-ray; 2.00 A; A=1-260.
DR PDB; 3OIK; X-ray; 1.50 A; A=1-260.
DR PDB; 3OIL; X-ray; 1.50 A; A=1-260.
DR PDB; 3OIM; X-ray; 1.45 A; A=1-260.
DR PDB; 3OKU; X-ray; 1.45 A; A=1-260.
DR PDB; 3OKV; X-ray; 1.45 A; A=1-260.
DR PDB; 3OY0; X-ray; 1.60 A; A=1-260.
DR PDB; 3OYQ; X-ray; 1.47 A; A=1-260.
DR PDB; 3OYS; X-ray; 1.54 A; A=1-260.
DR PDB; 3P3H; X-ray; 1.50 A; A=1-260.
DR PDB; 3P3J; X-ray; 1.60 A; A=1-260.
DR PDB; 3P44; X-ray; 2.20 A; A=1-260.
DR PDB; 3P4V; X-ray; 2.00 A; A=1-260.
DR PDB; 3P55; X-ray; 2.00 A; A=1-260.
DR PDB; 3P58; X-ray; 1.49 A; A=1-260.
DR PDB; 3P5A; X-ray; 1.49 A; A=1-260.
DR PDB; 3P5L; X-ray; 1.50 A; A=1-260.
DR PDB; 3PJJ; X-ray; 1.80 A; A=2-260.
DR PDB; 3PO6; X-ray; 1.47 A; A=2-260.
DR PDB; 3PYK; X-ray; 1.30 A; A=1-260.
DR PDB; 3QYK; X-ray; 1.47 A; A=1-260.
DR PDB; 3R16; X-ray; 1.60 A; A=4-260.
DR PDB; 3R17; X-ray; 1.70 A; B=4-260.
DR PDB; 3RG3; X-ray; 1.90 A; A=1-260.
DR PDB; 3RG4; X-ray; 1.50 A; A=1-260.
DR PDB; 3RGE; X-ray; 2.10 A; A=1-260.
DR PDB; 3RJ7; X-ray; 1.20 A; A=3-260.
DR PDB; 3RLD; X-ray; 1.50 A; A=1-260.
DR PDB; 3RYJ; X-ray; 1.39 A; B=2-260.
DR PDB; 3RYV; X-ray; 1.20 A; B=2-260.
DR PDB; 3RYX; X-ray; 1.60 A; B=2-260.
DR PDB; 3RYY; X-ray; 1.16 A; A=2-260.
DR PDB; 3RYZ; X-ray; 1.37 A; A=2-260.
DR PDB; 3RZ0; X-ray; 1.80 A; B=2-260.
DR PDB; 3RZ1; X-ray; 1.51 A; B=2-260.
DR PDB; 3RZ5; X-ray; 1.65 A; A=2-260.
DR PDB; 3RZ7; X-ray; 1.80 A; A=2-260.
DR PDB; 3RZ8; X-ray; 1.70 A; A=2-260.
DR PDB; 3S71; X-ray; 1.25 A; B=3-260.
DR PDB; 3S72; X-ray; 1.60 A; B=3-260.
DR PDB; 3S73; X-ray; 1.75 A; B=3-260.
DR PDB; 3S74; X-ray; 1.40 A; B=3-260.
DR PDB; 3S75; X-ray; 1.50 A; B=3-260.
DR PDB; 3S76; X-ray; 1.60 A; A=3-260.
DR PDB; 3S77; X-ray; 1.86 A; B=3-260.
DR PDB; 3S78; X-ray; 1.98 A; B=3-260.
DR PDB; 3S8X; X-ray; 1.30 A; A=1-260.
DR PDB; 3S9T; X-ray; 1.30 A; A=1-260.
DR PDB; 3SAP; X-ray; 1.75 A; A=1-260.
DR PDB; 3SAX; X-ray; 1.10 A; A=1-260.
DR PDB; 3SBH; X-ray; 1.65 A; A=1-260.
DR PDB; 3SBI; X-ray; 1.40 A; A=1-260.
DR PDB; 3T5U; X-ray; 1.75 A; A=2-260.
DR PDB; 3T5Z; X-ray; 1.65 A; A=2-260.
DR PDB; 3T82; X-ray; 2.00 A; A=1-260.
DR PDB; 3T83; X-ray; 1.80 A; A=1-260.
DR PDB; 3T84; X-ray; 2.00 A; A=1-260.
DR PDB; 3T85; X-ray; 2.40 A; A=1-260.
DR PDB; 3TMJ; Other; 2.00 A; A=3-260.
DR PDB; 3TVN; X-ray; 1.50 A; X=3-260.
DR PDB; 3TVO; X-ray; 1.60 A; X=3-260.
DR PDB; 3U3A; X-ray; 1.55 A; X=1-260.
DR PDB; 3U45; X-ray; 1.70 A; X=1-260.
DR PDB; 3U47; X-ray; 1.60 A; A=1-260.
DR PDB; 3U7C; X-ray; 0.93 A; A=1-260.
DR PDB; 3V2J; X-ray; 1.70 A; A=1-260.
DR PDB; 3V2M; X-ray; 1.47 A; A=1-260.
DR PDB; 3V3F; X-ray; 2.00 A; A=1-260.
DR PDB; 3V3G; X-ray; 1.56 A; B=1-260.
DR PDB; 3V3H; X-ray; 1.85 A; B=1-260.
DR PDB; 3V3I; X-ray; 1.73 A; B=1-260.
DR PDB; 3V3J; X-ray; 1.63 A; A=1-260.
DR PDB; 3V5G; X-ray; 1.50 A; A=1-260.
DR PDB; 3V7X; X-ray; 1.03 A; A=2-260.
DR PDB; 3VBD; X-ray; 1.05 A; A=2-260.
DR PDB; 3ZP9; X-ray; 1.31 A; A=1-260.
DR PDB; 4BCW; X-ray; 1.50 A; A=4-260.
DR PDB; 4BF1; X-ray; 1.35 A; A=2-260.
DR PDB; 4BF6; X-ray; 1.82 A; A=2-260.
DR PDB; 4CA2; X-ray; 2.10 A; A=1-260.
DR PDB; 4CAC; X-ray; 2.20 A; A=2-260.
DR PDB; 4CQ0; X-ray; 1.45 A; A=1-260.
DR PDB; 4DZ7; X-ray; 1.49 A; A=1-260.
DR PDB; 4DZ9; X-ray; 1.49 A; A=1-260.
DR PDB; 4E3D; X-ray; 1.60 A; A=1-260.
DR PDB; 4E3F; X-ray; 1.50 A; A=1-260.
DR PDB; 4E3G; X-ray; 1.55 A; A=1-260.
DR PDB; 4E3H; X-ray; 1.50 A; A=1-260.
DR PDB; 4E49; X-ray; 1.45 A; A=1-260.
DR PDB; 4E4A; X-ray; 1.45 A; A=1-260.
DR PDB; 4E5Q; X-ray; 1.70 A; A=1-260.
DR PDB; 4FIK; X-ray; 1.20 A; A=1-260.
DR PDB; 4FL7; X-ray; 1.85 A; A=2-260.
DR PDB; 4FPT; X-ray; 0.98 A; A=1-260.
DR PDB; 4FRC; X-ray; 0.98 A; A=1-260.
DR PDB; 4FU5; X-ray; 0.98 A; A=1-260.
DR PDB; 4FVN; X-ray; 1.05 A; A=1-260.
DR PDB; 4FVO; X-ray; 1.05 A; A=1-260.
DR PDB; 4G0C; Neutron; 2.00 A; A=4-260.
DR PDB; 4GL1; X-ray; 1.50 A; X=1-260.
DR PDB; 4HBA; X-ray; 1.76 A; A=1-260.
DR PDB; 4HEW; X-ray; 1.70 A; A=1-260.
DR PDB; 4HEY; X-ray; 1.45 A; A=1-260.
DR PDB; 4HEZ; X-ray; 1.34 A; A=1-260.
DR PDB; 4HF3; X-ray; 1.15 A; A=1-260.
DR PDB; 4HT0; X-ray; 1.60 A; A=1-260.
DR PDB; 4IDR; X-ray; 1.60 A; X=3-260.
DR PDB; 4ILX; X-ray; 1.60 A; A=4-260.
DR PDB; 4ITO; X-ray; 1.16 A; A=1-260.
DR PDB; 4ITP; X-ray; 1.70 A; A=4-260.
DR PDB; 4IWZ; X-ray; 1.60 A; A=4-260.
DR PDB; 4JS6; X-ray; 1.55 A; A=1-260.
DR PDB; 4JSA; X-ray; 1.50 A; A=1-260.
DR PDB; 4JSS; X-ray; 1.50 A; A=1-260.
DR PDB; 4JSW; X-ray; 1.90 A; A=1-260.
DR PDB; 4JSZ; X-ray; 1.90 A; A=1-260.
DR PDB; 4K0S; X-ray; 1.80 A; A=4-260.
DR PDB; 4K0T; X-ray; 1.78 A; A=4-260.
DR PDB; 4K0Z; X-ray; 1.80 A; A=3-260.
DR PDB; 4K13; X-ray; 1.60 A; A=4-260.
DR PDB; 4K1Q; X-ray; 1.70 A; A=3-260.
DR PDB; 4KAP; X-ray; 1.45 A; A=5-260.
DR PDB; 4KNI; X-ray; 1.80 A; A=1-260.
DR PDB; 4KNJ; X-ray; 2.00 A; A=1-260.
DR PDB; 4KUV; X-ray; 1.35 A; A=5-260.
DR PDB; 4KUW; X-ray; 1.55 A; A=4-260.
DR PDB; 4KUY; X-ray; 1.65 A; A=4-260.
DR PDB; 4KV0; X-ray; 1.55 A; A=4-260.
DR PDB; 4L5U; X-ray; 2.05 A; A=1-260.
DR PDB; 4L5V; X-ray; 1.63 A; A=1-260.
DR PDB; 4L5W; X-ray; 1.70 A; A=1-260.
DR PDB; 4LHI; X-ray; 1.60 A; A=1-260.
DR PDB; 4LP6; X-ray; 2.15 A; A/B=1-260.
DR PDB; 4M2R; X-ray; 1.99 A; A=4-260.
DR PDB; 4M2U; X-ray; 2.00 A; A=4-260.
DR PDB; 4M2V; X-ray; 1.72 A; A=4-260.
DR PDB; 4M2W; X-ray; 1.66 A; A=4-260.
DR PDB; 4MDG; X-ray; 1.35 A; A=3-260.
DR PDB; 4MDL; X-ray; 1.52 A; A=3-260.
DR PDB; 4MDM; X-ray; 1.55 A; A=3-260.
DR PDB; 4MLT; X-ray; 2.00 A; A=1-260.
DR PDB; 4MLX; X-ray; 1.65 A; A=1-260.
DR PDB; 4MO8; X-ray; 1.85 A; A=1-260.
DR PDB; 4MTY; X-ray; 1.00 A; A=1-260.
DR PDB; 4N0X; X-ray; 1.63 A; B=1-260.
DR PDB; 4N16; X-ray; 1.54 A; A=1-260.
DR PDB; 4PQ7; X-ray; 1.85 A; A=1-260.
DR PDB; 4PXX; X-ray; 1.85 A; A=1-260.
DR PDB; 4PYX; X-ray; 1.80 A; A=1-260.
DR PDB; 4PYY; X-ray; 1.75 A; A=1-260.
DR PDB; 4PZH; X-ray; 1.06 A; A=1-260.
DR PDB; 4Q06; X-ray; 1.15 A; A=1-260.
DR PDB; 4Q07; X-ray; 1.15 A; A=1-260.
DR PDB; 4Q08; X-ray; 1.07 A; A=1-260.
DR PDB; 4Q09; X-ray; 1.20 A; A=1-260.
DR PDB; 4Q49; Neutron; 1.80 A; A=1-260.
DR PDB; 4Q6D; X-ray; 1.12 A; A=1-260.
DR PDB; 4Q6E; X-ray; 1.12 A; A=1-260.
DR PDB; 4Q78; X-ray; 1.00 A; A=3-260.
DR PDB; 4Q7P; X-ray; 1.65 A; A=1-260.
DR PDB; 4Q7S; X-ray; 1.80 A; A=1-260.
DR PDB; 4Q7V; X-ray; 1.60 A; A=1-260.
DR PDB; 4Q7W; X-ray; 1.45 A; A=1-260.
DR PDB; 4Q81; X-ray; 1.55 A; A=1-260.
DR PDB; 4Q83; X-ray; 1.55 A; A=1-260.
DR PDB; 4Q87; X-ray; 1.55 A; A=1-260.
DR PDB; 4Q8X; X-ray; 1.55 A; A=1-260.
DR PDB; 4Q8Y; X-ray; 1.45 A; A=1-260.
DR PDB; 4Q8Z; X-ray; 1.50 A; A=1-260.
DR PDB; 4Q90; X-ray; 1.54 A; A=1-260.
DR PDB; 4Q99; X-ray; 1.50 A; A=1-260.
DR PDB; 4Q9Y; X-ray; 1.55 A; A=1-260.
DR PDB; 4QEF; X-ray; 1.47 A; A=1-260.
DR PDB; 4QIY; X-ray; 1.30 A; A/B/C/D=1-260.
DR PDB; 4QJM; X-ray; 1.75 A; A=1-260.
DR PDB; 4QK1; X-ray; 1.60 A; A=1-260.
DR PDB; 4QK2; X-ray; 1.52 A; A=1-260.
DR PDB; 4QK3; X-ray; 1.34 A; A=1-260.
DR PDB; 4QSA; X-ray; 1.50 A; A=1-260.
DR PDB; 4QSB; X-ray; 1.40 A; A=1-260.
DR PDB; 4QSI; X-ray; 1.95 A; A=1-260.
DR PDB; 4QTL; X-ray; 1.80 A; A=1-260.
DR PDB; 4QY3; X-ray; 1.50 A; A=2-260.
DR PDB; 4R59; X-ray; 1.65 A; A=1-260.
DR PDB; 4R5A; X-ray; 1.64 A; A=1-260.
DR PDB; 4R5B; X-ray; 1.50 A; A=1-260.
DR PDB; 4RFC; X-ray; 1.65 A; A=1-260.
DR PDB; 4RFD; X-ray; 1.63 A; A=1-260.
DR PDB; 4RH2; X-ray; 1.30 A; A=1-260.
DR PDB; 4RIU; X-ray; 1.65 A; A=1-260.
DR PDB; 4RIV; X-ray; 1.63 A; A=1-260.
DR PDB; 4RN4; X-ray; 1.53 A; A=1-260.
DR PDB; 4RUX; X-ray; 1.14 A; A=1-260.
DR PDB; 4RUY; X-ray; 1.14 A; A=1-260.
DR PDB; 4RUZ; X-ray; 1.63 A; A=1-260.
DR PDB; 4WL4; X-ray; 1.10 A; A=1-260.
DR PDB; 4WW6; X-ray; 1.06 A; A=1-260.
DR PDB; 4XE1; X-ray; 1.80 A; A=1-260.
DR PDB; 4Y0J; Neutron; 2.00 A; A=3-260.
DR PDB; 4YGJ; X-ray; 1.10 A; A=3-260.
DR PDB; 4YGK; X-ray; 1.50 A; A=3-260.
DR PDB; 4YGL; X-ray; 1.51 A; A=3-260.
DR PDB; 4YGN; X-ray; 1.23 A; A=3-260.
DR PDB; 4YVY; X-ray; 1.45 A; A=2-260.
DR PDB; 4YWP; X-ray; 1.45 A; A=4-260.
DR PDB; 4YX4; X-ray; 1.01 A; A=1-260.
DR PDB; 4YXI; X-ray; 0.96 A; A=1-260.
DR PDB; 4YXO; X-ray; 1.06 A; A=1-260.
DR PDB; 4YXU; X-ray; 1.08 A; A=1-260.
DR PDB; 4YYT; X-ray; 1.07 A; A=1-260.
DR PDB; 4Z0Q; X-ray; 1.45 A; A=3-260.
DR PDB; 4Z1E; X-ray; 2.01 A; A=2-260.
DR PDB; 4Z1J; X-ray; 1.27 A; A=3-260.
DR PDB; 4Z1K; X-ray; 1.35 A; A=4-260.
DR PDB; 4Z1N; X-ray; 1.47 A; A=3-260.
DR PDB; 4ZAO; X-ray; 1.80 A; A=1-257.
DR PDB; 4ZWI; X-ray; 1.60 A; A=4-260.
DR PDB; 4ZWX; X-ray; 1.70 A; A=4-260.
DR PDB; 4ZWY; X-ray; 1.50 A; A=4-260.
DR PDB; 4ZWZ; X-ray; 1.62 A; A=4-260.
DR PDB; 4ZX0; X-ray; 1.60 A; A=4-260.
DR PDB; 4ZX1; X-ray; 1.50 A; A=4-260.
DR PDB; 5A6H; X-ray; 1.57 A; A=1-260.
DR PDB; 5AMD; X-ray; 1.50 A; A=2-260.
DR PDB; 5AMG; X-ray; 1.55 A; A=2-260.
DR PDB; 5AML; X-ray; 1.36 A; A=2-260.
DR PDB; 5BNL; X-ray; 2.00 A; A=4-260.
DR PDB; 5BRU; X-ray; 1.60 A; A=3-260.
DR PDB; 5BRV; X-ray; 1.60 A; A=3-260.
DR PDB; 5BRW; X-ray; 1.40 A; A=1-260.
DR PDB; 5BYI; X-ray; 1.15 A; A=1-260.
DR PDB; 5C8I; Other; 1.56 A; A=1-260.
DR PDB; 5CA2; X-ray; 2.10 A; A=1-260.
DR PDB; 5CAC; X-ray; 2.20 A; A=2-260.
DR PDB; 5CLU; X-ray; 1.55 A; A=4-260.
DR PDB; 5DOG; X-ray; 1.70 A; A=1-260.
DR PDB; 5DOH; X-ray; 1.05 A; A/B=1-260.
DR PDB; 5DRS; X-ray; 1.10 A; A=1-260.
DR PDB; 5DSK; X-ray; 1.30 A; A=1-260.
DR PDB; 5DSL; X-ray; 1.45 A; A=1-260.
DR PDB; 5DSM; X-ray; 1.30 A; A=1-260.
DR PDB; 5DSO; X-ray; 1.40 A; A=1-260.
DR PDB; 5DSP; X-ray; 1.40 A; A=1-260.
DR PDB; 5DSQ; X-ray; 1.50 A; A=1-260.
DR PDB; 5DSR; X-ray; 1.30 A; A=1-260.
DR PDB; 5E28; X-ray; 1.30 A; A=4-260.
DR PDB; 5E2K; X-ray; 1.40 A; A=4-260.
DR PDB; 5E2R; X-ray; 1.60 A; A=1-260.
DR PDB; 5E2S; X-ray; 1.50 A; A=3-260.
DR PDB; 5EH5; X-ray; 1.21 A; A=1-260.
DR PDB; 5EH7; X-ray; 1.43 A; A=1-260.
DR PDB; 5EH8; X-ray; 1.38 A; A=1-260.
DR PDB; 5EHE; X-ray; 1.50 A; A=1-260.
DR PDB; 5EHV; X-ray; 1.21 A; A=1-260.
DR PDB; 5EHW; X-ray; 1.39 A; A=1-260.
DR PDB; 5EIJ; X-ray; 1.99 A; A=4-260.
DR PDB; 5EKH; X-ray; 1.34 A; A=1-260.
DR PDB; 5EKJ; X-ray; 1.13 A; A=1-260.
DR PDB; 5EKM; X-ray; 1.33 A; A=1-260.
DR PDB; 5EOI; X-ray; 1.80 A; A=3-260.
DR PDB; 5FDC; X-ray; 1.75 A; A=1-260.
DR PDB; 5FDI; X-ray; 1.85 A; A=1-260.
DR PDB; 5FLO; X-ray; 1.66 A; A=1-260.
DR PDB; 5FLP; X-ray; 1.71 A; A=1-260.
DR PDB; 5FLQ; X-ray; 1.70 A; A=1-260.
DR PDB; 5FLR; X-ray; 1.68 A; A=1-260.
DR PDB; 5FLS; X-ray; 1.67 A; A=1-260.
DR PDB; 5FLT; X-ray; 1.67 A; A=1-260.
DR PDB; 5FNG; X-ray; 2.05 A; A=1-260.
DR PDB; 5FNH; X-ray; 1.66 A; A=1-260.
DR PDB; 5FNI; X-ray; 1.60 A; A=1-260.
DR PDB; 5FNJ; X-ray; 1.67 A; A=1-260.
DR PDB; 5FNK; X-ray; 1.59 A; A=1-260.
DR PDB; 5FNL; X-ray; 1.59 A; A=1-260.
DR PDB; 5FNM; X-ray; 1.59 A; A=1-260.
DR PDB; 5G01; X-ray; 1.40 A; A=1-260.
DR PDB; 5G03; X-ray; 1.35 A; A=1-260.
DR PDB; 5G0B; X-ray; 1.55 A; A=1-260.
DR PDB; 5G0C; X-ray; 1.28 A; A=1-260.
DR PDB; 5GMN; X-ray; 1.80 A; A=1-260.
DR PDB; 5J8Z; X-ray; 1.70 A; A=1-260.
DR PDB; 5JDV; X-ray; 1.34 A; B=3-260.
DR PDB; 5JE7; X-ray; 1.15 A; B=4-260.
DR PDB; 5JEG; X-ray; 1.19 A; B=3-260.
DR PDB; 5JEH; X-ray; 1.13 A; B=3-260.
DR PDB; 5JEP; X-ray; 1.19 A; B=3-260.
DR PDB; 5JES; X-ray; 1.21 A; B=3-259.
DR PDB; 5JG3; X-ray; 1.21 A; B=3-260.
DR PDB; 5JG5; X-ray; 1.19 A; B=3-260.
DR PDB; 5JGS; X-ray; 1.11 A; B=4-260.
DR PDB; 5JGT; X-ray; 1.10 A; B=3-260.
DR PDB; 5JMZ; X-ray; 1.90 A; A=4-260.
DR PDB; 5JN3; X-ray; 1.60 A; A=4-260.
DR PDB; 5JN7; X-ray; 1.52 A; A=4-260.
DR PDB; 5JQ0; X-ray; 1.40 A; A=1-260.
DR PDB; 5JQT; X-ray; 1.36 A; A=1-260.
DR PDB; 5L3O; X-ray; 1.98 A; A/B=1-260.
DR PDB; 5L6K; X-ray; 1.70 A; A/B=1-260.
DR PDB; 5L6T; X-ray; 2.65 A; A/B=1-260.
DR PDB; 5L70; X-ray; 2.20 A; A/B=1-260.
DR PDB; 5L9E; X-ray; 2.90 A; A/B/C/D=1-260.
DR PDB; 5LJQ; X-ray; 1.05 A; A=3-260.
DR PDB; 5LJT; X-ray; 1.00 A; A=3-260.
DR PDB; 5LL4; X-ray; 1.12 A; A/B=1-260.
DR PDB; 5LL8; X-ray; 1.03 A; A=1-260.
DR PDB; 5LLC; X-ray; 1.10 A; A=1-260.
DR PDB; 5LLE; X-ray; 1.90 A; A=1-260.
DR PDB; 5LLG; X-ray; 1.12 A; A=1-260.
DR PDB; 5LLH; X-ray; 1.90 A; A=1-260.
DR PDB; 5LMD; X-ray; 1.70 A; A=1-260.
DR PDB; 5LVS; X-ray; 1.42 A; A/B=2-260.
DR PDB; 5M78; X-ray; 1.08 A; A=1-260.
DR PDB; 5MJN; X-ray; 1.17 A; A=2-260.
DR PDB; 5N0D; X-ray; 1.70 A; A=1-260.
DR PDB; 5N0E; X-ray; 1.75 A; A=1-260.
DR PDB; 5N1R; X-ray; 1.30 A; A=1-260.
DR PDB; 5N1S; X-ray; 1.30 A; A=1-260.
DR PDB; 5N24; X-ray; 1.50 A; A=1-260.
DR PDB; 5N25; X-ray; 1.40 A; A=1-260.
DR PDB; 5NEA; X-ray; 1.30 A; A=1-260.
DR PDB; 5NEE; X-ray; 1.70 A; A=1-260.
DR PDB; 5NXG; X-ray; 1.20 A; A=4-260.
DR PDB; 5NXI; X-ray; 1.16 A; A=3-260.
DR PDB; 5NXM; X-ray; 1.25 A; A=3-260.
DR PDB; 5NXO; X-ray; 1.20 A; A=3-260.
DR PDB; 5NXP; X-ray; 1.25 A; A=3-260.
DR PDB; 5NXV; X-ray; 1.10 A; A=3-260.
DR PDB; 5NXW; X-ray; 1.10 A; A=4-260.
DR PDB; 5NY1; X-ray; 1.10 A; A=4-260.
DR PDB; 5NY3; X-ray; 1.40 A; A=3-260.
DR PDB; 5NY6; X-ray; 1.10 A; A=3-260.
DR PDB; 5NYA; X-ray; 1.20 A; A=4-260.
DR PDB; 5O07; X-ray; 1.80 A; A=1-260.
DR PDB; 5OGN; X-ray; 1.10 A; A/B=3-260.
DR PDB; 5OGO; X-ray; 0.99 A; A=1-260.
DR PDB; 5OGP; X-ray; 1.10 A; A=2-260.
DR PDB; 5SZ0; X-ray; 1.63 A; A=4-260.
DR PDB; 5SZ1; X-ray; 1.55 A; A=4-260.
DR PDB; 5SZ2; X-ray; 1.63 A; A=4-260.
DR PDB; 5SZ3; X-ray; 1.69 A; A=4-260.
DR PDB; 5SZ4; X-ray; 1.60 A; A=4-260.
DR PDB; 5SZ5; X-ray; 1.27 A; A=4-260.
DR PDB; 5SZ6; X-ray; 1.15 A; A=4-260.
DR PDB; 5SZ7; X-ray; 1.78 A; A=4-260.
DR PDB; 5T71; X-ray; 1.30 A; A=1-260.
DR PDB; 5T72; X-ray; 1.30 A; A=1-260.
DR PDB; 5T74; X-ray; 1.20 A; A=1-260.
DR PDB; 5T75; X-ray; 1.50 A; A=1-260.
DR PDB; 5TFX; X-ray; 1.50 A; A=1-260.
DR PDB; 5TH4; X-ray; 1.47 A; A=1-260.
DR PDB; 5THI; X-ray; 1.50 A; A=1-260.
DR PDB; 5THJ; X-ray; 1.50 A; A=1-260.
DR PDB; 5THN; X-ray; 1.33 A; A=1-260.
DR PDB; 5TI0; X-ray; 1.42 A; A=1-260.
DR PDB; 5TXY; X-ray; 1.21 A; A=1-260.
DR PDB; 5TY1; X-ray; 1.60 A; A=1-260.
DR PDB; 5TY8; X-ray; 1.45 A; A=1-260.
DR PDB; 5TY9; X-ray; 1.53 A; A=1-260.
DR PDB; 5TYA; X-ray; 1.50 A; A=1-260.
DR PDB; 5U0D; X-ray; 1.59 A; A=1-260.
DR PDB; 5U0E; X-ray; 1.27 A; A=1-260.
DR PDB; 5U0F; X-ray; 1.21 A; A=1-260.
DR PDB; 5U0G; X-ray; 1.54 A; A=1-260.
DR PDB; 5ULN; X-ray; 1.35 A; A=1-260.
DR PDB; 5UMC; X-ray; 2.15 A; A=1-260.
DR PDB; 5VGY; X-ray; 1.39 A; A=1-260.
DR PDB; 5W8B; X-ray; 1.60 A; A=4-260.
DR PDB; 5WEX; X-ray; 1.26 A; A=1-260.
DR PDB; 5WG7; X-ray; 1.45 A; A=4-260.
DR PDB; 5WGP; X-ray; 1.53 A; A=4-260.
DR PDB; 5WLR; X-ray; 1.49 A; A=4-260.
DR PDB; 5WLT; X-ray; 1.57 A; A=4-260.
DR PDB; 5WLU; X-ray; 1.39 A; A=4-260.
DR PDB; 5WLV; X-ray; 1.40 A; A=4-260.
DR PDB; 5Y2R; X-ray; 1.00 A; A=1-260.
DR PDB; 5Y2S; X-ray; 0.90 A; A=1-260.
DR PDB; 5YUI; X-ray; 1.20 A; A=1-260.
DR PDB; 5YUJ; X-ray; 1.25 A; A=1-260.
DR PDB; 5YUK; X-ray; 1.45 A; A=1-260.
DR PDB; 5ZXW; X-ray; 1.32 A; A=5-260.
DR PDB; 6B4D; X-ray; 1.20 A; A=4-260.
DR PDB; 6B59; X-ray; 1.64 A; A=4-260.
DR PDB; 6B5A; X-ray; 1.62 A; A=4-260.
DR PDB; 6BBS; Other; 2.00 A; A=1-260.
DR PDB; 6BC9; Other; 1.80 A; A=1-260.
DR PDB; 6BCC; Other; 1.80 A; A=1-260.
DR PDB; 6C7W; X-ray; 1.28 A; A=1-260.
DR PDB; 6C7X; X-ray; 1.50 A; A=1-260.
DR PDB; 6CA2; X-ray; 2.50 A; A=1-260.
DR PDB; 6CEH; X-ray; 1.43 A; A=2-260.
DR PDB; 6CJV; X-ray; 1.55 A; A=4-260.
DR PDB; 6D1L; X-ray; 1.40 A; A=1-260.
DR PDB; 6D1M; X-ray; 1.21 A; A=1-260.
DR PDB; 6E8P; X-ray; 1.90 A; A=4-260.
DR PDB; 6E8X; X-ray; 1.60 A; A=4-260.
DR PDB; 6E91; X-ray; 1.80 A; A=4-260.
DR PDB; 6E92; X-ray; 1.77 A; A=4-260.
DR PDB; 6EBE; X-ray; 1.88 A; A=4-260.
DR PDB; 6ECZ; X-ray; 2.21 A; A=4-260.
DR PDB; 6EDA; X-ray; 1.88 A; A=4-260.
DR PDB; 6EEA; X-ray; 1.63 A; A=4-260.
DR PDB; 6EEH; X-ray; 1.63 A; A=4-260.
DR PDB; 6EEO; X-ray; 1.72 A; A=4-260.
DR PDB; 6EQU; X-ray; 1.65 A; A=1-260.
DR PDB; 6FJI; Other; 1.60 A; A=1-260.
DR PDB; 6FJJ; Other; 1.50 A; A=1-260.
DR PDB; 6G3Q; X-ray; 1.01 A; A=1-260.
DR PDB; 6G6T; X-ray; 1.12 A; A=1-260.
DR PDB; 6GCY; Other; 1.30 A; A=1-260.
DR PDB; 6GDC; X-ray; 1.08 A; A=1-260.
DR PDB; 6GM9; X-ray; 1.09 A; A=1-260.
DR PDB; 6GOT; X-ray; 1.56 A; A=1-260.
DR PDB; 6GXB; X-ray; 1.35 A; A=4-260.
DR PDB; 6GXE; X-ray; 1.30 A; A=4-260.
DR PDB; 6H29; X-ray; 1.46 A; A=1-260.
DR PDB; 6H2Z; X-ray; 1.94 A; A=1-260.
DR PDB; 6H33; X-ray; 1.58 A; A=1-260.
DR PDB; 6H34; X-ray; 1.55 A; A=1-260.
DR PDB; 6H3Q; X-ray; 1.31 A; A=1-260.
DR PDB; 6H6S; X-ray; 1.45 A; A/B=2-260.
DR PDB; 6HD2; NMR; -; A=1-260.
DR PDB; 6HQX; X-ray; 1.10 A; A=1-260.
DR PDB; 6HR3; X-ray; 1.02 A; A=1-260.
DR PDB; 6HX5; X-ray; 1.44 A; A=1-260.
DR PDB; 6HXD; X-ray; 1.12 A; A=1-260.
DR PDB; 6HZX; X-ray; 2.91 A; A/B=4-260.
DR PDB; 6I0W; X-ray; 1.04 A; A=1-260.
DR PDB; 6I1U; X-ray; 1.08 A; A=1-260.
DR PDB; 6I2F; X-ray; 1.20 A; A=1-260.
DR PDB; 6I3E; X-ray; 1.07 A; A=1-260.
DR PDB; 6IC2; X-ray; 1.15 A; A=1-260.
DR PDB; 6KLZ; X-ray; 0.90 A; A=1-260.
DR PDB; 6KM0; X-ray; 0.93 A; A=1-260.
DR PDB; 6KM1; X-ray; 1.05 A; A=1-260.
DR PDB; 6KM2; X-ray; 0.90 A; A=1-260.
DR PDB; 6KM3; X-ray; 1.15 A; A=1-260.
DR PDB; 6KM4; X-ray; 1.15 A; A=1-260.
DR PDB; 6KM5; X-ray; 1.15 A; A=1-260.
DR PDB; 6KM6; X-ray; 1.15 A; A=1-260.
DR PDB; 6LUU; X-ray; 1.20 A; A=1-260.
DR PDB; 6LUV; X-ray; 1.20 A; A=1-260.
DR PDB; 6LUW; X-ray; 1.20 A; A=1-260.
DR PDB; 6LUX; X-ray; 1.20 A; A=1-260.
DR PDB; 6LUY; X-ray; 1.20 A; A=1-260.
DR PDB; 6LUZ; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV1; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV2; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV3; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV4; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV5; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV6; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV7; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV8; X-ray; 1.20 A; A=1-260.
DR PDB; 6LV9; X-ray; 1.20 A; A=1-260.
DR PDB; 6LVA; X-ray; 1.20 A; A=1-260.
DR PDB; 6MBV; X-ray; 1.70 A; A=4-260.
DR PDB; 6MBY; X-ray; 1.50 A; A=4-260.
DR PDB; 6NLV; X-ray; 1.79 A; A=4-260.
DR PDB; 6NM0; X-ray; 1.44 A; A=4-260.
DR PDB; 6ODZ; X-ray; 1.30 A; A=1-260.
DR PDB; 6OE0; X-ray; 1.30 A; A=1-260.
DR PDB; 6OE1; X-ray; 1.45 A; A=1-260.
DR PDB; 6OTI; X-ray; 2.00 A; A=4-260.
DR PDB; 6OTK; X-ray; 1.12 A; A=4-260.
DR PDB; 6OTM; X-ray; 1.31 A; A=4-260.
DR PDB; 6OTO; X-ray; 1.50 A; A=1-260.
DR PDB; 6OTP; X-ray; 1.47 A; A=4-260.
DR PDB; 6OTQ; X-ray; 1.47 A; A=4-260.
DR PDB; 6OUB; X-ray; 1.42 A; A=4-260.
DR PDB; 6OUD; X-ray; 1.26 A; A=4-260.
DR PDB; 6OUE; X-ray; 1.42 A; A=4-260.
DR PDB; 6OUF; X-ray; 1.36 A; A=4-260.
DR PDB; 6OUH; X-ray; 1.45 A; A=4-260.
DR PDB; 6OUI; X-ray; 1.53 A; A=4-260.
DR PDB; 6OUJ; X-ray; 1.47 A; A=4-260.
DR PDB; 6OUK; X-ray; 1.50 A; A=4-260.
DR PDB; 6OUM; X-ray; 1.56 A; A=4-260.
DR PDB; 6PDV; X-ray; 1.23 A; A=1-260.
DR PDB; 6PEA; X-ray; 1.36 A; A=1-260.
DR PDB; 6PGX; X-ray; 1.36 A; A=1-260.
DR PDB; 6Q3O; X-ray; 2.23 A; A/B/C/D=2-260.
DR PDB; 6Q9T; X-ray; 2.68 A; A=2-260.
DR PDB; 6QEB; NMR; -; A=1-260.
DR PDB; 6QL1; X-ray; 1.42 A; A=1-260.
DR PDB; 6QL2; X-ray; 1.30 A; A=1-260.
DR PDB; 6QL3; X-ray; 1.35 A; A=1-260.
DR PDB; 6R6F; X-ray; 1.20 A; A=1-260.
DR PDB; 6R6J; X-ray; 1.55 A; A=1-260.
DR PDB; 6RFH; X-ray; 0.97 A; A=1-260.
DR PDB; 6RG3; X-ray; 1.32 A; A=1-260.
DR PDB; 6RG4; X-ray; 1.25 A; A=1-260.
DR PDB; 6RG5; X-ray; 1.09 A; A=1-260.
DR PDB; 6RH4; X-ray; 0.95 A; A=1-260.
DR PDB; 6RHJ; X-ray; 1.44 A; A=1-260.
DR PDB; 6RHK; X-ray; 1.44 A; A=1-260.
DR PDB; 6RIG; X-ray; 1.00 A; A=1-260.
DR PDB; 6RIT; X-ray; 1.01 A; A=1-260.
DR PDB; 6RJJ; X-ray; 1.06 A; A=1-260.
DR PDB; 6RKN; X-ray; 0.96 A; A=1-260.
DR PDB; 6RL9; X-ray; 1.00 A; A=1-260.
DR PDB; 6RM1; X-ray; 1.68 A; A=1-260.
DR PDB; 6RMP; X-ray; 1.22 A; A=1-260.
DR PDB; 6RMX; X-ray; 1.60 A; A=4-260.
DR PDB; 6RMY; X-ray; 1.50 A; A=1-260.
DR PDB; 6RNP; X-ray; 1.07 A; A=1-260.
DR PDB; 6ROB; X-ray; 0.93 A; A=1-260.
DR PDB; 6ROE; X-ray; 0.94 A; A=1-260.
DR PDB; 6ROF; X-ray; 1.50 A; A=1-260.
DR PDB; 6RQI; X-ray; 0.95 A; A=1-260.
DR PDB; 6RRG; X-ray; 1.13 A; A=1-260.
DR PDB; 6RRI; X-ray; 1.10 A; A=1-260.
DR PDB; 6RS5; X-ray; 1.07 A; A=1-260.
DR PDB; 6RSZ; X-ray; 1.09 A; A=1-260.
DR PDB; 6RVF; X-ray; 2.07 A; A=1-260.
DR PDB; 6RVK; X-ray; 1.58 A; A=1-260.
DR PDB; 6RVL; X-ray; 1.72 A; A=1-260.
DR PDB; 6RW1; X-ray; 1.70 A; A=1-260.
DR PDB; 6RZX; X-ray; 1.00 A; A=1-260.
DR PDB; 6S03; X-ray; 1.38 A; A=1-260.
DR PDB; 6S9G; X-ray; 1.14 A; A=1-260.
DR PDB; 6S9Z; X-ray; 0.95 A; A=1-260.
DR PDB; 6SAC; X-ray; 1.02 A; A=1-260.
DR PDB; 6SAS; X-ray; 1.10 A; A=1-260.
DR PDB; 6SAY; X-ray; 0.95 A; A=1-260.
DR PDB; 6SB7; X-ray; 1.09 A; A=1-260.
DR PDB; 6SBH; X-ray; 0.95 A; A=1-260.
DR PDB; 6SBL; X-ray; 0.94 A; A=1-260.
DR PDB; 6SBM; X-ray; 0.95 A; A=1-260.
DR PDB; 6SD7; X-ray; 1.05 A; A=1-260.
DR PDB; 6SDH; X-ray; 1.04 A; A=1-260.
DR PDB; 6SDI; X-ray; 1.03 A; A=1-260.
DR PDB; 6SDJ; X-ray; 1.02 A; A=1-260.
DR PDB; 6SDL; X-ray; 1.08 A; A=1-260.
DR PDB; 6SDS; X-ray; 1.26 A; A=1-260.
DR PDB; 6SEY; X-ray; 1.23 A; A=1-260.
DR PDB; 6SFQ; X-ray; 1.00 A; A=1-260.
DR PDB; 6SFU; X-ray; 1.04 A; A=1-260.
DR PDB; 6SG0; X-ray; 1.13 A; A=1-260.
DR PDB; 6SG6; X-ray; 0.98 A; A=1-260.
DR PDB; 6SX9; X-ray; 1.43 A; A=1-260.
DR PDB; 6SYB; X-ray; 1.60 A; A=1-260.
DR PDB; 6SYS; X-ray; 1.30 A; A=1-260.
DR PDB; 6T4N; X-ray; 1.40 A; A=1-260.
DR PDB; 6T4O; X-ray; 1.13 A; A=1-260.
DR PDB; 6T4P; X-ray; 1.75 A; A=1-260.
DR PDB; 6T5C; X-ray; 1.22 A; A=1-260.
DR PDB; 6T7U; X-ray; 1.20 A; A=1-260.
DR PDB; 6T81; X-ray; 0.98 A; A=1-260.
DR PDB; 6T9Z; X-ray; 1.12 A; A=1-260.
DR PDB; 6U4Q; X-ray; 1.31 A; A=4-260.
DR PDB; 6U4T; X-ray; 1.36 A; A=4-260.
DR PDB; 6UFB; X-ray; 1.67 A; A=1-260.
DR PDB; 6UFC; X-ray; 1.32 A; A=1-260.
DR PDB; 6UFD; X-ray; 1.48 A; A=1-260.
DR PDB; 6UGN; X-ray; 1.41 A; A=4-260.
DR PDB; 6UGO; X-ray; 1.46 A; A=4-260.
DR PDB; 6UGP; X-ray; 1.31 A; A=4-260.
DR PDB; 6UGQ; X-ray; 1.30 A; A=4-260.
DR PDB; 6UGR; X-ray; 1.31 A; A=4-260.
DR PDB; 6UGZ; X-ray; 1.31 A; A=4-260.
DR PDB; 6UH0; X-ray; 1.31 A; A=4-260.
DR PDB; 6UX1; X-ray; 1.36 A; A=1-260.
DR PDB; 6UZU; X-ray; 1.50 A; A=4-260.
DR PDB; 6VJ3; X-ray; 1.35 A; A=3-260.
DR PDB; 6VKG; X-ray; 1.37 A; A=1-260.
DR PDB; 6WKA; X-ray; 1.34 A; A=1-260.
DR PDB; 6WQ4; X-ray; 1.35 A; A=1-260.
DR PDB; 6WQ5; X-ray; 1.30 A; A=1-260.
DR PDB; 6WQ7; X-ray; 1.30 A; A=1-260.
DR PDB; 6WQ8; X-ray; 1.41 A; A=1-260.
DR PDB; 6WQ9; X-ray; 1.30 A; A=1-260.
DR PDB; 6XVH; X-ray; 1.80 A; A=4-260.
DR PDB; 6XWZ; X-ray; 1.38 A; AAA=1-260.
DR PDB; 6XXT; X-ray; 1.05 A; X=1-260.
DR PDB; 6YH4; X-ray; 1.30 A; A=1-260.
DR PDB; 6YH5; X-ray; 1.20 A; A=1-260.
DR PDB; 6YH6; X-ray; 1.40 A; A=1-260.
DR PDB; 6YH7; X-ray; 1.12 A; A=1-260.
DR PDB; 6YH8; X-ray; 1.20 A; A=1-260.
DR PDB; 6YH9; X-ray; 1.55 A; A=1-260.
DR PDB; 6YHA; X-ray; 1.25 A; A=1-260.
DR PDB; 6YHB; X-ray; 1.65 A; A=1-260.
DR PDB; 6YHC; X-ray; 1.28 A; A=1-260.
DR PDB; 6YJ3; X-ray; 1.55 A; A=1-260.
DR PDB; 6YKC; X-ray; 1.20 A; A=1-260.
DR PDB; 6YKH; X-ray; 1.10 A; A=1-260.
DR PDB; 6YMA; EM; 2.50 A; A=1-260.
DR PDB; 6YMB; EM; 2.50 A; A=1-260.
DR PDB; 6YO2; X-ray; 1.20 A; A=1-260.
DR PDB; 6YO4; X-ray; 1.70 A; A=1-260.
DR PDB; 6YO7; X-ray; 1.17 A; A=1-260.
DR PDB; 6YOI; X-ray; 1.20 A; A=1-260.
DR PDB; 6YOK; X-ray; 1.25 A; A=1-260.
DR PDB; 6YOL; X-ray; 1.15 A; A=1-260.
DR PDB; 6YPW; X-ray; 1.10 A; A=1-260.
DR PDB; 6YQT; X-ray; 1.50 A; A=1-260.
DR PDB; 6YQU; X-ray; 1.48 A; A=1-260.
DR PDB; 6YRI; X-ray; 1.60 A; A=1-260.
DR PDB; 6YZJ; X-ray; 1.20 A; A=1-260.
DR PDB; 6YZK; X-ray; 0.99 A; A=1-260.
DR PDB; 6YZL; X-ray; 1.20 A; A=1-260.
DR PDB; 6YZM; X-ray; 1.50 A; A=1-260.
DR PDB; 6YZN; X-ray; 0.95 A; A=1-260.
DR PDB; 6YZO; X-ray; 1.50 A; A=1-260.
DR PDB; 6YZP; X-ray; 1.35 A; A=1-260.
DR PDB; 6YZQ; X-ray; 1.04 A; A=1-260.
DR PDB; 6YZR; X-ray; 1.20 A; A=1-260.
DR PDB; 6YZS; X-ray; 1.05 A; A=1-260.
DR PDB; 6YZT; X-ray; 1.05 A; A=1-260.
DR PDB; 6YZU; X-ray; 1.00 A; A=1-260.
DR PDB; 6YZV; X-ray; 1.65 A; A=1-260.
DR PDB; 6YZW; X-ray; 1.03 A; A=1-260.
DR PDB; 6YZX; X-ray; 1.10 A; A=1-260.
DR PDB; 6Z04; X-ray; 1.05 A; A=1-260.
DR PDB; 6ZR8; X-ray; 1.79 A; A=1-260.
DR PDB; 7A6V; X-ray; 2.00 A; A=3-260.
DR PDB; 7AEQ; X-ray; 1.50 A; A=1-260.
DR PDB; 7AES; X-ray; 1.40 A; A=1-260.
DR PDB; 7AGN; X-ray; 1.15 A; A/B/C/D=1-260.
DR PDB; 7ASJ; X-ray; 1.43 A; A=1-260.
DR PDB; 7BFA; X-ray; 1.60 A; AAA=1-260.
DR PDB; 7BG5; X-ray; 1.43 A; AAA=1-260.
DR PDB; 7BHH; X-ray; 1.40 A; A=1-260.
DR PDB; 7BI5; X-ray; 1.74 A; A=1-260.
DR PDB; 7CA2; X-ray; 2.40 A; A=1-260.
DR PDB; 7JNR; X-ray; 1.44 A; A=1-260.
DR PDB; 7JNV; X-ray; 1.49 A; A=1-260.
DR PDB; 7JNW; X-ray; 1.29 A; A=1-260.
DR PDB; 7JNX; X-ray; 1.29 A; A=1-260.
DR PDB; 7JNZ; X-ray; 1.29 A; A=1-260.
DR PDB; 7JO0; X-ray; 1.61 A; A=1-257.
DR PDB; 7JO1; X-ray; 1.50 A; A=1-257.
DR PDB; 7JO2; X-ray; 1.31 A; A=1-257.
DR PDB; 7JO3; X-ray; 1.45 A; A=1-257.
DR PDB; 7JOB; X-ray; 1.38 A; A=1-257.
DR PDB; 7JOC; X-ray; 1.39 A; A=1-257.
DR PDB; 7K6I; X-ray; 1.41 A; A=1-260.
DR PDB; 7K6J; X-ray; 1.75 A; A=1-260.
DR PDB; 7K6K; X-ray; 1.31 A; A=1-260.
DR PDB; 7K6L; X-ray; 1.66 A; A=1-260.
DR PDB; 7K6T; X-ray; 1.76 A; A=1-257.
DR PDB; 7K6U; X-ray; 1.60 A; A=1-257.
DR PDB; 7K6X; X-ray; 1.76 A; A=1-257.
DR PDB; 7K6Z; X-ray; 1.66 A; A=1-257.
DR PDB; 7M23; X-ray; 1.30 A; A=3-260.
DR PDB; 7M24; X-ray; 1.30 A; A=3-260.
DR PDB; 7M26; X-ray; 1.30 A; A=3-260.
DR PDB; 7MU3; X-ray; 1.35 A; A=1-260.
DR PDB; 7NH6; X-ray; 1.28 A; AAA=1-260.
DR PDB; 7NH8; X-ray; 1.37 A; AAA=1-260.
DR PDB; 7NTB; X-ray; 1.70 A; A=2-260.
DR PDB; 7NZR; X-ray; 1.28 A; A=1-260.
DR PDB; 7NZS; X-ray; 1.50 A; A=1-260.
DR PDB; 7NZT; X-ray; 1.35 A; A=1-260.
DR PDB; 7NZU; X-ray; 1.24 A; A=1-260.
DR PDB; 7NZW; X-ray; 1.45 A; A=1-260.
DR PDB; 7NZX; X-ray; 1.33 A; A=1-260.
DR PDB; 7ONV; X-ray; 1.04 A; AAA=1-260.
DR PDB; 7Q0C; X-ray; 1.12 A; A/B=1-260.
DR PDB; 7Q0E; X-ray; 1.30 A; A=3-260.
DR PDB; 7QBH; X-ray; 1.22 A; AAA=1-260.
DR PDB; 7SUW; X-ray; 1.46 A; A=4-260.
DR PDB; 7SUY; X-ray; 1.41 A; A=4-260.
DR PDB; 7SV1; X-ray; 1.56 A; A=4-260.
DR PDB; 7SV8; X-ray; 1.39 A; A=4-260.
DR PDB; 8CA2; X-ray; 2.40 A; A=1-260.
DR PDB; 9CA2; X-ray; 2.80 A; A=1-260.
DR PDBsum; 12CA; -.
DR PDBsum; 1A42; -.
DR PDBsum; 1AM6; -.
DR PDBsum; 1AVN; -.
DR PDBsum; 1BCD; -.
DR PDBsum; 1BIC; -.
DR PDBsum; 1BN1; -.
DR PDBsum; 1BN3; -.
DR PDBsum; 1BN4; -.
DR PDBsum; 1BNM; -.
DR PDBsum; 1BNN; -.
DR PDBsum; 1BNQ; -.
DR PDBsum; 1BNT; -.
DR PDBsum; 1BNU; -.
DR PDBsum; 1BNV; -.
DR PDBsum; 1BNW; -.
DR PDBsum; 1BV3; -.
DR PDBsum; 1CA2; -.
DR PDBsum; 1CA3; -.
DR PDBsum; 1CAH; -.
DR PDBsum; 1CAI; -.
DR PDBsum; 1CAJ; -.
DR PDBsum; 1CAK; -.
DR PDBsum; 1CAL; -.
DR PDBsum; 1CAM; -.
DR PDBsum; 1CAN; -.
DR PDBsum; 1CAO; -.
DR PDBsum; 1CAY; -.
DR PDBsum; 1CAZ; -.
DR PDBsum; 1CCS; -.
DR PDBsum; 1CCT; -.
DR PDBsum; 1CCU; -.
DR PDBsum; 1CIL; -.
DR PDBsum; 1CIM; -.
DR PDBsum; 1CIN; -.
DR PDBsum; 1CNB; -.
DR PDBsum; 1CNC; -.
DR PDBsum; 1CNG; -.
DR PDBsum; 1CNH; -.
DR PDBsum; 1CNI; -.
DR PDBsum; 1CNJ; -.
DR PDBsum; 1CNK; -.
DR PDBsum; 1CNW; -.
DR PDBsum; 1CNX; -.
DR PDBsum; 1CNY; -.
DR PDBsum; 1CRA; -.
DR PDBsum; 1CVA; -.
DR PDBsum; 1CVB; -.
DR PDBsum; 1CVC; -.
DR PDBsum; 1CVD; -.
DR PDBsum; 1CVE; -.
DR PDBsum; 1CVF; -.
DR PDBsum; 1CVH; -.
DR PDBsum; 1DCA; -.
DR PDBsum; 1DCB; -.
DR PDBsum; 1EOU; -.
DR PDBsum; 1F2W; -.
DR PDBsum; 1FQL; -.
DR PDBsum; 1FQM; -.
DR PDBsum; 1FQN; -.
DR PDBsum; 1FQR; -.
DR PDBsum; 1FR4; -.
DR PDBsum; 1FR7; -.
DR PDBsum; 1FSN; -.
DR PDBsum; 1FSQ; -.
DR PDBsum; 1FSR; -.
DR PDBsum; 1G0E; -.
DR PDBsum; 1G0F; -.
DR PDBsum; 1G1D; -.
DR PDBsum; 1G3Z; -.
DR PDBsum; 1G45; -.
DR PDBsum; 1G46; -.
DR PDBsum; 1G48; -.
DR PDBsum; 1G4J; -.
DR PDBsum; 1G4O; -.
DR PDBsum; 1G52; -.
DR PDBsum; 1G53; -.
DR PDBsum; 1G54; -.
DR PDBsum; 1H4N; -.
DR PDBsum; 1H9N; -.
DR PDBsum; 1H9Q; -.
DR PDBsum; 1HCA; -.
DR PDBsum; 1HEA; -.
DR PDBsum; 1HEB; -.
DR PDBsum; 1HEC; -.
DR PDBsum; 1HED; -.
DR PDBsum; 1HVA; -.
DR PDBsum; 1I8Z; -.
DR PDBsum; 1I90; -.
DR PDBsum; 1I91; -.
DR PDBsum; 1I9L; -.
DR PDBsum; 1I9M; -.
DR PDBsum; 1I9N; -.
DR PDBsum; 1I9O; -.
DR PDBsum; 1I9P; -.
DR PDBsum; 1I9Q; -.
DR PDBsum; 1IF4; -.
DR PDBsum; 1IF5; -.
DR PDBsum; 1IF6; -.
DR PDBsum; 1IF7; -.
DR PDBsum; 1IF8; -.
DR PDBsum; 1IF9; -.
DR PDBsum; 1KWQ; -.
DR PDBsum; 1KWR; -.
DR PDBsum; 1LG5; -.
DR PDBsum; 1LG6; -.
DR PDBsum; 1LGD; -.
DR PDBsum; 1LUG; -.
DR PDBsum; 1LZV; -.
DR PDBsum; 1MOO; -.
DR PDBsum; 1MUA; -.
DR PDBsum; 1OKL; -.
DR PDBsum; 1OKM; -.
DR PDBsum; 1OKN; -.
DR PDBsum; 1OQ5; -.
DR PDBsum; 1RAY; -.
DR PDBsum; 1RAZ; -.
DR PDBsum; 1RZA; -.
DR PDBsum; 1RZB; -.
DR PDBsum; 1RZC; -.
DR PDBsum; 1RZD; -.
DR PDBsum; 1RZE; -.
DR PDBsum; 1T9N; -.
DR PDBsum; 1TB0; -.
DR PDBsum; 1TBT; -.
DR PDBsum; 1TE3; -.
DR PDBsum; 1TEQ; -.
DR PDBsum; 1TEU; -.
DR PDBsum; 1TG3; -.
DR PDBsum; 1TG9; -.
DR PDBsum; 1TH9; -.
DR PDBsum; 1THK; -.
DR PDBsum; 1TTM; -.
DR PDBsum; 1UGA; -.
DR PDBsum; 1UGB; -.
DR PDBsum; 1UGC; -.
DR PDBsum; 1UGD; -.
DR PDBsum; 1UGE; -.
DR PDBsum; 1UGF; -.
DR PDBsum; 1UGG; -.
DR PDBsum; 1XEG; -.
DR PDBsum; 1XEV; -.
DR PDBsum; 1XPZ; -.
DR PDBsum; 1XQ0; -.
DR PDBsum; 1YDA; -.
DR PDBsum; 1YDB; -.
DR PDBsum; 1YDC; -.
DR PDBsum; 1YDD; -.
DR PDBsum; 1YO0; -.
DR PDBsum; 1YO1; -.
DR PDBsum; 1YO2; -.
DR PDBsum; 1Z9Y; -.
DR PDBsum; 1ZE8; -.
DR PDBsum; 1ZFK; -.
DR PDBsum; 1ZFQ; -.
DR PDBsum; 1ZGE; -.
DR PDBsum; 1ZGF; -.
DR PDBsum; 1ZH9; -.
DR PDBsum; 1ZSA; -.
DR PDBsum; 1ZSB; -.
DR PDBsum; 1ZSC; -.
DR PDBsum; 2ABE; -.
DR PDBsum; 2AW1; -.
DR PDBsum; 2AX2; -.
DR PDBsum; 2CA2; -.
DR PDBsum; 2CBA; -.
DR PDBsum; 2CBB; -.
DR PDBsum; 2CBC; -.
DR PDBsum; 2CBD; -.
DR PDBsum; 2CBE; -.
DR PDBsum; 2EU2; -.
DR PDBsum; 2EU3; -.
DR PDBsum; 2EZ7; -.
DR PDBsum; 2F14; -.
DR PDBsum; 2FMG; -.
DR PDBsum; 2FMZ; -.
DR PDBsum; 2FNK; -.
DR PDBsum; 2FNM; -.
DR PDBsum; 2FNN; -.
DR PDBsum; 2FOQ; -.
DR PDBsum; 2FOS; -.
DR PDBsum; 2FOU; -.
DR PDBsum; 2FOV; -.
DR PDBsum; 2GD8; -.
DR PDBsum; 2GEH; -.
DR PDBsum; 2H15; -.
DR PDBsum; 2H4N; -.
DR PDBsum; 2HD6; -.
DR PDBsum; 2HKK; -.
DR PDBsum; 2HL4; -.
DR PDBsum; 2HNC; -.
DR PDBsum; 2HOC; -.
DR PDBsum; 2ILI; -.
DR PDBsum; 2NNG; -.
DR PDBsum; 2NNO; -.
DR PDBsum; 2NNS; -.
DR PDBsum; 2NNV; -.
DR PDBsum; 2NWO; -.
DR PDBsum; 2NWP; -.
DR PDBsum; 2NWY; -.
DR PDBsum; 2NWZ; -.
DR PDBsum; 2NXR; -.
DR PDBsum; 2NXS; -.
DR PDBsum; 2NXT; -.
DR PDBsum; 2O4Z; -.
DR PDBsum; 2OSF; -.
DR PDBsum; 2OSM; -.
DR PDBsum; 2POU; -.
DR PDBsum; 2POV; -.
DR PDBsum; 2POW; -.
DR PDBsum; 2Q1B; -.
DR PDBsum; 2Q1Q; -.
DR PDBsum; 2Q38; -.
DR PDBsum; 2QO8; -.
DR PDBsum; 2QOA; -.
DR PDBsum; 2QP6; -.
DR PDBsum; 2VVA; -.
DR PDBsum; 2VVB; -.
DR PDBsum; 2WD2; -.
DR PDBsum; 2WD3; -.
DR PDBsum; 2WEG; -.
DR PDBsum; 2WEH; -.
DR PDBsum; 2WEJ; -.
DR PDBsum; 2WEO; -.
DR PDBsum; 2X7S; -.
DR PDBsum; 2X7T; -.
DR PDBsum; 2X7U; -.
DR PDBsum; 3B4F; -.
DR PDBsum; 3BET; -.
DR PDBsum; 3BL0; -.
DR PDBsum; 3BL1; -.
DR PDBsum; 3C7P; -.
DR PDBsum; 3CA2; -.
DR PDBsum; 3CAJ; -.
DR PDBsum; 3CYU; -.
DR PDBsum; 3D8W; -.
DR PDBsum; 3D92; -.
DR PDBsum; 3D93; -.
DR PDBsum; 3D9Z; -.
DR PDBsum; 3DAZ; -.
DR PDBsum; 3DBU; -.
DR PDBsum; 3DC3; -.
DR PDBsum; 3DC9; -.
DR PDBsum; 3DCC; -.
DR PDBsum; 3DCS; -.
DR PDBsum; 3DCW; -.
DR PDBsum; 3DD0; -.
DR PDBsum; 3DD8; -.
DR PDBsum; 3DV7; -.
DR PDBsum; 3DVB; -.
DR PDBsum; 3DVC; -.
DR PDBsum; 3DVD; -.
DR PDBsum; 3EFI; -.
DR PDBsum; 3EFT; -.
DR PDBsum; 3F4X; -.
DR PDBsum; 3F8E; -.
DR PDBsum; 3FFP; -.
DR PDBsum; 3GZ0; -.
DR PDBsum; 3HFP; -.
DR PDBsum; 3HKN; -.
DR PDBsum; 3HKQ; -.
DR PDBsum; 3HKT; -.
DR PDBsum; 3HKU; -.
DR PDBsum; 3HLJ; -.
DR PDBsum; 3HS4; -.
DR PDBsum; 3IBI; -.
DR PDBsum; 3IBL; -.
DR PDBsum; 3IBN; -.
DR PDBsum; 3IBU; -.
DR PDBsum; 3IEO; -.
DR PDBsum; 3IGP; -.
DR PDBsum; 3K2F; -.
DR PDBsum; 3K34; -.
DR PDBsum; 3K7K; -.
DR PDBsum; 3KIG; -.
DR PDBsum; 3KKX; -.
DR PDBsum; 3KNE; -.
DR PDBsum; 3KOI; -.
DR PDBsum; 3KOK; -.
DR PDBsum; 3KON; -.
DR PDBsum; 3KS3; -.
DR PDBsum; 3KWA; -.
DR PDBsum; 3L14; -.
DR PDBsum; 3M04; -.
DR PDBsum; 3M14; -.
DR PDBsum; 3M1J; -.
DR PDBsum; 3M1K; -.
DR PDBsum; 3M1Q; -.
DR PDBsum; 3M1W; -.
DR PDBsum; 3M2N; -.
DR PDBsum; 3M2X; -.
DR PDBsum; 3M2Y; -.
DR PDBsum; 3M2Z; -.
DR PDBsum; 3M3X; -.
DR PDBsum; 3M40; -.
DR PDBsum; 3M5E; -.
DR PDBsum; 3M5S; -.
DR PDBsum; 3M5T; -.
DR PDBsum; 3M67; -.
DR PDBsum; 3M96; -.
DR PDBsum; 3M98; -.
DR PDBsum; 3MHC; -.
DR PDBsum; 3MHI; -.
DR PDBsum; 3MHL; -.
DR PDBsum; 3MHM; -.
DR PDBsum; 3MHO; -.
DR PDBsum; 3ML2; -.
DR PDBsum; 3MMF; -.
DR PDBsum; 3MNA; -.
DR PDBsum; 3MNH; -.
DR PDBsum; 3MNI; -.
DR PDBsum; 3MNJ; -.
DR PDBsum; 3MNK; -.
DR PDBsum; 3MNU; -.
DR PDBsum; 3MWO; -.
DR PDBsum; 3MYQ; -.
DR PDBsum; 3MZC; -.
DR PDBsum; 3N0N; -.
DR PDBsum; 3N2P; -.
DR PDBsum; 3N3J; -.
DR PDBsum; 3N4B; -.
DR PDBsum; 3NB5; -.
DR PDBsum; 3NI5; -.
DR PDBsum; 3NJ9; -.
DR PDBsum; 3OIK; -.
DR PDBsum; 3OIL; -.
DR PDBsum; 3OIM; -.
DR PDBsum; 3OKU; -.
DR PDBsum; 3OKV; -.
DR PDBsum; 3OY0; -.
DR PDBsum; 3OYQ; -.
DR PDBsum; 3OYS; -.
DR PDBsum; 3P3H; -.
DR PDBsum; 3P3J; -.
DR PDBsum; 3P44; -.
DR PDBsum; 3P4V; -.
DR PDBsum; 3P55; -.
DR PDBsum; 3P58; -.
DR PDBsum; 3P5A; -.
DR PDBsum; 3P5L; -.
DR PDBsum; 3PJJ; -.
DR PDBsum; 3PO6; -.
DR PDBsum; 3PYK; -.
DR PDBsum; 3QYK; -.
DR PDBsum; 3R16; -.
DR PDBsum; 3R17; -.
DR PDBsum; 3RG3; -.
DR PDBsum; 3RG4; -.
DR PDBsum; 3RGE; -.
DR PDBsum; 3RJ7; -.
DR PDBsum; 3RLD; -.
DR PDBsum; 3RYJ; -.
DR PDBsum; 3RYV; -.
DR PDBsum; 3RYX; -.
DR PDBsum; 3RYY; -.
DR PDBsum; 3RYZ; -.
DR PDBsum; 3RZ0; -.
DR PDBsum; 3RZ1; -.
DR PDBsum; 3RZ5; -.
DR PDBsum; 3RZ7; -.
DR PDBsum; 3RZ8; -.
DR PDBsum; 3S71; -.
DR PDBsum; 3S72; -.
DR PDBsum; 3S73; -.
DR PDBsum; 3S74; -.
DR PDBsum; 3S75; -.
DR PDBsum; 3S76; -.
DR PDBsum; 3S77; -.
DR PDBsum; 3S78; -.
DR PDBsum; 3S8X; -.
DR PDBsum; 3S9T; -.
DR PDBsum; 3SAP; -.
DR PDBsum; 3SAX; -.
DR PDBsum; 3SBH; -.
DR PDBsum; 3SBI; -.
DR PDBsum; 3T5U; -.
DR PDBsum; 3T5Z; -.
DR PDBsum; 3T82; -.
DR PDBsum; 3T83; -.
DR PDBsum; 3T84; -.
DR PDBsum; 3T85; -.
DR PDBsum; 3TMJ; -.
DR PDBsum; 3TVN; -.
DR PDBsum; 3TVO; -.
DR PDBsum; 3U3A; -.
DR PDBsum; 3U45; -.
DR PDBsum; 3U47; -.
DR PDBsum; 3U7C; -.
DR PDBsum; 3V2J; -.
DR PDBsum; 3V2M; -.
DR PDBsum; 3V3F; -.
DR PDBsum; 3V3G; -.
DR PDBsum; 3V3H; -.
DR PDBsum; 3V3I; -.
DR PDBsum; 3V3J; -.
DR PDBsum; 3V5G; -.
DR PDBsum; 3V7X; -.
DR PDBsum; 3VBD; -.
DR PDBsum; 3ZP9; -.
DR PDBsum; 4BCW; -.
DR PDBsum; 4BF1; -.
DR PDBsum; 4BF6; -.
DR PDBsum; 4CA2; -.
DR PDBsum; 4CAC; -.
DR PDBsum; 4CQ0; -.
DR PDBsum; 4DZ7; -.
DR PDBsum; 4DZ9; -.
DR PDBsum; 4E3D; -.
DR PDBsum; 4E3F; -.
DR PDBsum; 4E3G; -.
DR PDBsum; 4E3H; -.
DR PDBsum; 4E49; -.
DR PDBsum; 4E4A; -.
DR PDBsum; 4E5Q; -.
DR PDBsum; 4FIK; -.
DR PDBsum; 4FL7; -.
DR PDBsum; 4FPT; -.
DR PDBsum; 4FRC; -.
DR PDBsum; 4FU5; -.
DR PDBsum; 4FVN; -.
DR PDBsum; 4FVO; -.
DR PDBsum; 4G0C; -.
DR PDBsum; 4GL1; -.
DR PDBsum; 4HBA; -.
DR PDBsum; 4HEW; -.
DR PDBsum; 4HEY; -.
DR PDBsum; 4HEZ; -.
DR PDBsum; 4HF3; -.
DR PDBsum; 4HT0; -.
DR PDBsum; 4IDR; -.
DR PDBsum; 4ILX; -.
DR PDBsum; 4ITO; -.
DR PDBsum; 4ITP; -.
DR PDBsum; 4IWZ; -.
DR PDBsum; 4JS6; -.
DR PDBsum; 4JSA; -.
DR PDBsum; 4JSS; -.
DR PDBsum; 4JSW; -.
DR PDBsum; 4JSZ; -.
DR PDBsum; 4K0S; -.
DR PDBsum; 4K0T; -.
DR PDBsum; 4K0Z; -.
DR PDBsum; 4K13; -.
DR PDBsum; 4K1Q; -.
DR PDBsum; 4KAP; -.
DR PDBsum; 4KNI; -.
DR PDBsum; 4KNJ; -.
DR PDBsum; 4KUV; -.
DR PDBsum; 4KUW; -.
DR PDBsum; 4KUY; -.
DR PDBsum; 4KV0; -.
DR PDBsum; 4L5U; -.
DR PDBsum; 4L5V; -.
DR PDBsum; 4L5W; -.
DR PDBsum; 4LHI; -.
DR PDBsum; 4LP6; -.
DR PDBsum; 4M2R; -.
DR PDBsum; 4M2U; -.
DR PDBsum; 4M2V; -.
DR PDBsum; 4M2W; -.
DR PDBsum; 4MDG; -.
DR PDBsum; 4MDL; -.
DR PDBsum; 4MDM; -.
DR PDBsum; 4MLT; -.
DR PDBsum; 4MLX; -.
DR PDBsum; 4MO8; -.
DR PDBsum; 4MTY; -.
DR PDBsum; 4N0X; -.
DR PDBsum; 4N16; -.
DR PDBsum; 4PQ7; -.
DR PDBsum; 4PXX; -.
DR PDBsum; 4PYX; -.
DR PDBsum; 4PYY; -.
DR PDBsum; 4PZH; -.
DR PDBsum; 4Q06; -.
DR PDBsum; 4Q07; -.
DR PDBsum; 4Q08; -.
DR PDBsum; 4Q09; -.
DR PDBsum; 4Q49; -.
DR PDBsum; 4Q6D; -.
DR PDBsum; 4Q6E; -.
DR PDBsum; 4Q78; -.
DR PDBsum; 4Q7P; -.
DR PDBsum; 4Q7S; -.
DR PDBsum; 4Q7V; -.
DR PDBsum; 4Q7W; -.
DR PDBsum; 4Q81; -.
DR PDBsum; 4Q83; -.
DR PDBsum; 4Q87; -.
DR PDBsum; 4Q8X; -.
DR PDBsum; 4Q8Y; -.
DR PDBsum; 4Q8Z; -.
DR PDBsum; 4Q90; -.
DR PDBsum; 4Q99; -.
DR PDBsum; 4Q9Y; -.
DR PDBsum; 4QEF; -.
DR PDBsum; 4QIY; -.
DR PDBsum; 4QJM; -.
DR PDBsum; 4QK1; -.
DR PDBsum; 4QK2; -.
DR PDBsum; 4QK3; -.
DR PDBsum; 4QSA; -.
DR PDBsum; 4QSB; -.
DR PDBsum; 4QSI; -.
DR PDBsum; 4QTL; -.
DR PDBsum; 4QY3; -.
DR PDBsum; 4R59; -.
DR PDBsum; 4R5A; -.
DR PDBsum; 4R5B; -.
DR PDBsum; 4RFC; -.
DR PDBsum; 4RFD; -.
DR PDBsum; 4RH2; -.
DR PDBsum; 4RIU; -.
DR PDBsum; 4RIV; -.
DR PDBsum; 4RN4; -.
DR PDBsum; 4RUX; -.
DR PDBsum; 4RUY; -.
DR PDBsum; 4RUZ; -.
DR PDBsum; 4WL4; -.
DR PDBsum; 4WW6; -.
DR PDBsum; 4XE1; -.
DR PDBsum; 4Y0J; -.
DR PDBsum; 4YGJ; -.
DR PDBsum; 4YGK; -.
DR PDBsum; 4YGL; -.
DR PDBsum; 4YGN; -.
DR PDBsum; 4YVY; -.
DR PDBsum; 4YWP; -.
DR PDBsum; 4YX4; -.
DR PDBsum; 4YXI; -.
DR PDBsum; 4YXO; -.
DR PDBsum; 4YXU; -.
DR PDBsum; 4YYT; -.
DR PDBsum; 4Z0Q; -.
DR PDBsum; 4Z1E; -.
DR PDBsum; 4Z1J; -.
DR PDBsum; 4Z1K; -.
DR PDBsum; 4Z1N; -.
DR PDBsum; 4ZAO; -.
DR PDBsum; 4ZWI; -.
DR PDBsum; 4ZWX; -.
DR PDBsum; 4ZWY; -.
DR PDBsum; 4ZWZ; -.
DR PDBsum; 4ZX0; -.
DR PDBsum; 4ZX1; -.
DR PDBsum; 5A6H; -.
DR PDBsum; 5AMD; -.
DR PDBsum; 5AMG; -.
DR PDBsum; 5AML; -.
DR PDBsum; 5BNL; -.
DR PDBsum; 5BRU; -.
DR PDBsum; 5BRV; -.
DR PDBsum; 5BRW; -.
DR PDBsum; 5BYI; -.
DR PDBsum; 5C8I; -.
DR PDBsum; 5CA2; -.
DR PDBsum; 5CAC; -.
DR PDBsum; 5CLU; -.
DR PDBsum; 5DOG; -.
DR PDBsum; 5DOH; -.
DR PDBsum; 5DRS; -.
DR PDBsum; 5DSK; -.
DR PDBsum; 5DSL; -.
DR PDBsum; 5DSM; -.
DR PDBsum; 5DSO; -.
DR PDBsum; 5DSP; -.
DR PDBsum; 5DSQ; -.
DR PDBsum; 5DSR; -.
DR PDBsum; 5E28; -.
DR PDBsum; 5E2K; -.
DR PDBsum; 5E2R; -.
DR PDBsum; 5E2S; -.
DR PDBsum; 5EH5; -.
DR PDBsum; 5EH7; -.
DR PDBsum; 5EH8; -.
DR PDBsum; 5EHE; -.
DR PDBsum; 5EHV; -.
DR PDBsum; 5EHW; -.
DR PDBsum; 5EIJ; -.
DR PDBsum; 5EKH; -.
DR PDBsum; 5EKJ; -.
DR PDBsum; 5EKM; -.
DR PDBsum; 5EOI; -.
DR PDBsum; 5FDC; -.
DR PDBsum; 5FDI; -.
DR PDBsum; 5FLO; -.
DR PDBsum; 5FLP; -.
DR PDBsum; 5FLQ; -.
DR PDBsum; 5FLR; -.
DR PDBsum; 5FLS; -.
DR PDBsum; 5FLT; -.
DR PDBsum; 5FNG; -.
DR PDBsum; 5FNH; -.
DR PDBsum; 5FNI; -.
DR PDBsum; 5FNJ; -.
DR PDBsum; 5FNK; -.
DR PDBsum; 5FNL; -.
DR PDBsum; 5FNM; -.
DR PDBsum; 5G01; -.
DR PDBsum; 5G03; -.
DR PDBsum; 5G0B; -.
DR PDBsum; 5G0C; -.
DR PDBsum; 5GMN; -.
DR PDBsum; 5J8Z; -.
DR PDBsum; 5JDV; -.
DR PDBsum; 5JE7; -.
DR PDBsum; 5JEG; -.
DR PDBsum; 5JEH; -.
DR PDBsum; 5JEP; -.
DR PDBsum; 5JES; -.
DR PDBsum; 5JG3; -.
DR PDBsum; 5JG5; -.
DR PDBsum; 5JGS; -.
DR PDBsum; 5JGT; -.
DR PDBsum; 5JMZ; -.
DR PDBsum; 5JN3; -.
DR PDBsum; 5JN7; -.
DR PDBsum; 5JQ0; -.
DR PDBsum; 5JQT; -.
DR PDBsum; 5L3O; -.
DR PDBsum; 5L6K; -.
DR PDBsum; 5L6T; -.
DR PDBsum; 5L70; -.
DR PDBsum; 5L9E; -.
DR PDBsum; 5LJQ; -.
DR PDBsum; 5LJT; -.
DR PDBsum; 5LL4; -.
DR PDBsum; 5LL8; -.
DR PDBsum; 5LLC; -.
DR PDBsum; 5LLE; -.
DR PDBsum; 5LLG; -.
DR PDBsum; 5LLH; -.
DR PDBsum; 5LMD; -.
DR PDBsum; 5LVS; -.
DR PDBsum; 5M78; -.
DR PDBsum; 5MJN; -.
DR PDBsum; 5N0D; -.
DR PDBsum; 5N0E; -.
DR PDBsum; 5N1R; -.
DR PDBsum; 5N1S; -.
DR PDBsum; 5N24; -.
DR PDBsum; 5N25; -.
DR PDBsum; 5NEA; -.
DR PDBsum; 5NEE; -.
DR PDBsum; 5NXG; -.
DR PDBsum; 5NXI; -.
DR PDBsum; 5NXM; -.
DR PDBsum; 5NXO; -.
DR PDBsum; 5NXP; -.
DR PDBsum; 5NXV; -.
DR PDBsum; 5NXW; -.
DR PDBsum; 5NY1; -.
DR PDBsum; 5NY3; -.
DR PDBsum; 5NY6; -.
DR PDBsum; 5NYA; -.
DR PDBsum; 5O07; -.
DR PDBsum; 5OGN; -.
DR PDBsum; 5OGO; -.
DR PDBsum; 5OGP; -.
DR PDBsum; 5SZ0; -.
DR PDBsum; 5SZ1; -.
DR PDBsum; 5SZ2; -.
DR PDBsum; 5SZ3; -.
DR PDBsum; 5SZ4; -.
DR PDBsum; 5SZ5; -.
DR PDBsum; 5SZ6; -.
DR PDBsum; 5SZ7; -.
DR PDBsum; 5T71; -.
DR PDBsum; 5T72; -.
DR PDBsum; 5T74; -.
DR PDBsum; 5T75; -.
DR PDBsum; 5TFX; -.
DR PDBsum; 5TH4; -.
DR PDBsum; 5THI; -.
DR PDBsum; 5THJ; -.
DR PDBsum; 5THN; -.
DR PDBsum; 5TI0; -.
DR PDBsum; 5TXY; -.
DR PDBsum; 5TY1; -.
DR PDBsum; 5TY8; -.
DR PDBsum; 5TY9; -.
DR PDBsum; 5TYA; -.
DR PDBsum; 5U0D; -.
DR PDBsum; 5U0E; -.
DR PDBsum; 5U0F; -.
DR PDBsum; 5U0G; -.
DR PDBsum; 5ULN; -.
DR PDBsum; 5UMC; -.
DR PDBsum; 5VGY; -.
DR PDBsum; 5W8B; -.
DR PDBsum; 5WEX; -.
DR PDBsum; 5WG7; -.
DR PDBsum; 5WGP; -.
DR PDBsum; 5WLR; -.
DR PDBsum; 5WLT; -.
DR PDBsum; 5WLU; -.
DR PDBsum; 5WLV; -.
DR PDBsum; 5Y2R; -.
DR PDBsum; 5Y2S; -.
DR PDBsum; 5YUI; -.
DR PDBsum; 5YUJ; -.
DR PDBsum; 5YUK; -.
DR PDBsum; 5ZXW; -.
DR PDBsum; 6B4D; -.
DR PDBsum; 6B59; -.
DR PDBsum; 6B5A; -.
DR PDBsum; 6BBS; -.
DR PDBsum; 6BC9; -.
DR PDBsum; 6BCC; -.
DR PDBsum; 6C7W; -.
DR PDBsum; 6C7X; -.
DR PDBsum; 6CA2; -.
DR PDBsum; 6CEH; -.
DR PDBsum; 6CJV; -.
DR PDBsum; 6D1L; -.
DR PDBsum; 6D1M; -.
DR PDBsum; 6E8P; -.
DR PDBsum; 6E8X; -.
DR PDBsum; 6E91; -.
DR PDBsum; 6E92; -.
DR PDBsum; 6EBE; -.
DR PDBsum; 6ECZ; -.
DR PDBsum; 6EDA; -.
DR PDBsum; 6EEA; -.
DR PDBsum; 6EEH; -.
DR PDBsum; 6EEO; -.
DR PDBsum; 6EQU; -.
DR PDBsum; 6FJI; -.
DR PDBsum; 6FJJ; -.
DR PDBsum; 6G3Q; -.
DR PDBsum; 6G6T; -.
DR PDBsum; 6GCY; -.
DR PDBsum; 6GDC; -.
DR PDBsum; 6GM9; -.
DR PDBsum; 6GOT; -.
DR PDBsum; 6GXB; -.
DR PDBsum; 6GXE; -.
DR PDBsum; 6H29; -.
DR PDBsum; 6H2Z; -.
DR PDBsum; 6H33; -.
DR PDBsum; 6H34; -.
DR PDBsum; 6H3Q; -.
DR PDBsum; 6H6S; -.
DR PDBsum; 6HD2; -.
DR PDBsum; 6HQX; -.
DR PDBsum; 6HR3; -.
DR PDBsum; 6HX5; -.
DR PDBsum; 6HXD; -.
DR PDBsum; 6HZX; -.
DR PDBsum; 6I0W; -.
DR PDBsum; 6I1U; -.
DR PDBsum; 6I2F; -.
DR PDBsum; 6I3E; -.
DR PDBsum; 6IC2; -.
DR PDBsum; 6KLZ; -.
DR PDBsum; 6KM0; -.
DR PDBsum; 6KM1; -.
DR PDBsum; 6KM2; -.
DR PDBsum; 6KM3; -.
DR PDBsum; 6KM4; -.
DR PDBsum; 6KM5; -.
DR PDBsum; 6KM6; -.
DR PDBsum; 6LUU; -.
DR PDBsum; 6LUV; -.
DR PDBsum; 6LUW; -.
DR PDBsum; 6LUX; -.
DR PDBsum; 6LUY; -.
DR PDBsum; 6LUZ; -.
DR PDBsum; 6LV1; -.
DR PDBsum; 6LV2; -.
DR PDBsum; 6LV3; -.
DR PDBsum; 6LV4; -.
DR PDBsum; 6LV5; -.
DR PDBsum; 6LV6; -.
DR PDBsum; 6LV7; -.
DR PDBsum; 6LV8; -.
DR PDBsum; 6LV9; -.
DR PDBsum; 6LVA; -.
DR PDBsum; 6MBV; -.
DR PDBsum; 6MBY; -.
DR PDBsum; 6NLV; -.
DR PDBsum; 6NM0; -.
DR PDBsum; 6ODZ; -.
DR PDBsum; 6OE0; -.
DR PDBsum; 6OE1; -.
DR PDBsum; 6OTI; -.
DR PDBsum; 6OTK; -.
DR PDBsum; 6OTM; -.
DR PDBsum; 6OTO; -.
DR PDBsum; 6OTP; -.
DR PDBsum; 6OTQ; -.
DR PDBsum; 6OUB; -.
DR PDBsum; 6OUD; -.
DR PDBsum; 6OUE; -.
DR PDBsum; 6OUF; -.
DR PDBsum; 6OUH; -.
DR PDBsum; 6OUI; -.
DR PDBsum; 6OUJ; -.
DR PDBsum; 6OUK; -.
DR PDBsum; 6OUM; -.
DR PDBsum; 6PDV; -.
DR PDBsum; 6PEA; -.
DR PDBsum; 6PGX; -.
DR PDBsum; 6Q3O; -.
DR PDBsum; 6Q9T; -.
DR PDBsum; 6QEB; -.
DR PDBsum; 6QL1; -.
DR PDBsum; 6QL2; -.
DR PDBsum; 6QL3; -.
DR PDBsum; 6R6F; -.
DR PDBsum; 6R6J; -.
DR PDBsum; 6RFH; -.
DR PDBsum; 6RG3; -.
DR PDBsum; 6RG4; -.
DR PDBsum; 6RG5; -.
DR PDBsum; 6RH4; -.
DR PDBsum; 6RHJ; -.
DR PDBsum; 6RHK; -.
DR PDBsum; 6RIG; -.
DR PDBsum; 6RIT; -.
DR PDBsum; 6RJJ; -.
DR PDBsum; 6RKN; -.
DR PDBsum; 6RL9; -.
DR PDBsum; 6RM1; -.
DR PDBsum; 6RMP; -.
DR PDBsum; 6RMX; -.
DR PDBsum; 6RMY; -.
DR PDBsum; 6RNP; -.
DR PDBsum; 6ROB; -.
DR PDBsum; 6ROE; -.
DR PDBsum; 6ROF; -.
DR PDBsum; 6RQI; -.
DR PDBsum; 6RRG; -.
DR PDBsum; 6RRI; -.
DR PDBsum; 6RS5; -.
DR PDBsum; 6RSZ; -.
DR PDBsum; 6RVF; -.
DR PDBsum; 6RVK; -.
DR PDBsum; 6RVL; -.
DR PDBsum; 6RW1; -.
DR PDBsum; 6RZX; -.
DR PDBsum; 6S03; -.
DR PDBsum; 6S9G; -.
DR PDBsum; 6S9Z; -.
DR PDBsum; 6SAC; -.
DR PDBsum; 6SAS; -.
DR PDBsum; 6SAY; -.
DR PDBsum; 6SB7; -.
DR PDBsum; 6SBH; -.
DR PDBsum; 6SBL; -.
DR PDBsum; 6SBM; -.
DR PDBsum; 6SD7; -.
DR PDBsum; 6SDH; -.
DR PDBsum; 6SDI; -.
DR PDBsum; 6SDJ; -.
DR PDBsum; 6SDL; -.
DR PDBsum; 6SDS; -.
DR PDBsum; 6SEY; -.
DR PDBsum; 6SFQ; -.
DR PDBsum; 6SFU; -.
DR PDBsum; 6SG0; -.
DR PDBsum; 6SG6; -.
DR PDBsum; 6SX9; -.
DR PDBsum; 6SYB; -.
DR PDBsum; 6SYS; -.
DR PDBsum; 6T4N; -.
DR PDBsum; 6T4O; -.
DR PDBsum; 6T4P; -.
DR PDBsum; 6T5C; -.
DR PDBsum; 6T7U; -.
DR PDBsum; 6T81; -.
DR PDBsum; 6T9Z; -.
DR PDBsum; 6U4Q; -.
DR PDBsum; 6U4T; -.
DR PDBsum; 6UFB; -.
DR PDBsum; 6UFC; -.
DR PDBsum; 6UFD; -.
DR PDBsum; 6UGN; -.
DR PDBsum; 6UGO; -.
DR PDBsum; 6UGP; -.
DR PDBsum; 6UGQ; -.
DR PDBsum; 6UGR; -.
DR PDBsum; 6UGZ; -.
DR PDBsum; 6UH0; -.
DR PDBsum; 6UX1; -.
DR PDBsum; 6UZU; -.
DR PDBsum; 6VJ3; -.
DR PDBsum; 6VKG; -.
DR PDBsum; 6WKA; -.
DR PDBsum; 6WQ4; -.
DR PDBsum; 6WQ5; -.
DR PDBsum; 6WQ7; -.
DR PDBsum; 6WQ8; -.
DR PDBsum; 6WQ9; -.
DR PDBsum; 6XVH; -.
DR PDBsum; 6XWZ; -.
DR PDBsum; 6XXT; -.
DR PDBsum; 6YH4; -.
DR PDBsum; 6YH5; -.
DR PDBsum; 6YH6; -.
DR PDBsum; 6YH7; -.
DR PDBsum; 6YH8; -.
DR PDBsum; 6YH9; -.
DR PDBsum; 6YHA; -.
DR PDBsum; 6YHB; -.
DR PDBsum; 6YHC; -.
DR PDBsum; 6YJ3; -.
DR PDBsum; 6YKC; -.
DR PDBsum; 6YKH; -.
DR PDBsum; 6YMA; -.
DR PDBsum; 6YMB; -.
DR PDBsum; 6YO2; -.
DR PDBsum; 6YO4; -.
DR PDBsum; 6YO7; -.
DR PDBsum; 6YOI; -.
DR PDBsum; 6YOK; -.
DR PDBsum; 6YOL; -.
DR PDBsum; 6YPW; -.
DR PDBsum; 6YQT; -.
DR PDBsum; 6YQU; -.
DR PDBsum; 6YRI; -.
DR PDBsum; 6YZJ; -.
DR PDBsum; 6YZK; -.
DR PDBsum; 6YZL; -.
DR PDBsum; 6YZM; -.
DR PDBsum; 6YZN; -.
DR PDBsum; 6YZO; -.
DR PDBsum; 6YZP; -.
DR PDBsum; 6YZQ; -.
DR PDBsum; 6YZR; -.
DR PDBsum; 6YZS; -.
DR PDBsum; 6YZT; -.
DR PDBsum; 6YZU; -.
DR PDBsum; 6YZV; -.
DR PDBsum; 6YZW; -.
DR PDBsum; 6YZX; -.
DR PDBsum; 6Z04; -.
DR PDBsum; 6ZR8; -.
DR PDBsum; 7A6V; -.
DR PDBsum; 7AEQ; -.
DR PDBsum; 7AES; -.
DR PDBsum; 7AGN; -.
DR PDBsum; 7ASJ; -.
DR PDBsum; 7BFA; -.
DR PDBsum; 7BG5; -.
DR PDBsum; 7BHH; -.
DR PDBsum; 7BI5; -.
DR PDBsum; 7CA2; -.
DR PDBsum; 7JNR; -.
DR PDBsum; 7JNV; -.
DR PDBsum; 7JNW; -.
DR PDBsum; 7JNX; -.
DR PDBsum; 7JNZ; -.
DR PDBsum; 7JO0; -.
DR PDBsum; 7JO1; -.
DR PDBsum; 7JO2; -.
DR PDBsum; 7JO3; -.
DR PDBsum; 7JOB; -.
DR PDBsum; 7JOC; -.
DR PDBsum; 7K6I; -.
DR PDBsum; 7K6J; -.
DR PDBsum; 7K6K; -.
DR PDBsum; 7K6L; -.
DR PDBsum; 7K6T; -.
DR PDBsum; 7K6U; -.
DR PDBsum; 7K6X; -.
DR PDBsum; 7K6Z; -.
DR PDBsum; 7M23; -.
DR PDBsum; 7M24; -.
DR PDBsum; 7M26; -.
DR PDBsum; 7MU3; -.
DR PDBsum; 7NH6; -.
DR PDBsum; 7NH8; -.
DR PDBsum; 7NTB; -.
DR PDBsum; 7NZR; -.
DR PDBsum; 7NZS; -.
DR PDBsum; 7NZT; -.
DR PDBsum; 7NZU; -.
DR PDBsum; 7NZW; -.
DR PDBsum; 7NZX; -.
DR PDBsum; 7ONV; -.
DR PDBsum; 7Q0C; -.
DR PDBsum; 7Q0E; -.
DR PDBsum; 7QBH; -.
DR PDBsum; 7SUW; -.
DR PDBsum; 7SUY; -.
DR PDBsum; 7SV1; -.
DR PDBsum; 7SV8; -.
DR PDBsum; 8CA2; -.
DR PDBsum; 9CA2; -.
DR AlphaFoldDB; P00918; -.
DR SMR; P00918; -.
DR BioGRID; 107215; 41.
DR IntAct; P00918; 14.
DR MINT; P00918; -.
DR STRING; 9606.ENSP00000285379; -.
DR BindingDB; P00918; -.
DR ChEMBL; CHEMBL205; -.
DR DrugBank; DB07596; (17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamate.
DR DrugBank; DB03333; (4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester.
DR DrugBank; DB08418; (4aS,4bR,10bS,12aS)-12a-methyl-1,3-dioxo-2-(pyridin-3-ylmethyl)-1,2,3,4,4a,4b,5,6,10b,11,12,12a-dodecahydronaphtho[2,1-f]isoquinolin-8-yl sulfamate.
DR DrugBank; DB04081; (4s-Trans)-4-(Methylamino)-5,6-Dihydro-6-Methyl-4h-Thieno(2,3-B)Thiopyran-2-Sulfonamide-7,7-Dioxide.
DR DrugBank; DB08416; (9BETA,13ALPHA,14BETA,17ALPHA)-2-METHOXYESTRA-1,3,5(10)-TRIENE-3,17-DIYL DISULFAMATE.
DR DrugBank; DB02479; (R)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide.
DR DrugBank; DB07467; (S)-Indapamide.
DR DrugBank; DB03950; (S)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide.
DR DrugBank; DB03594; 1,2,4-Triazole.
DR DrugBank; DB03294; 1-Methyl-3-Oxo-1,3-Dihydro-Benzo[C]Isothiazole-5-Sulfonic Acid Amide.
DR DrugBank; DB04763; 1-N-(4-SULFAMOYLPHENYL-ETHYL)-2,4,6-TRIMETHYLPYRIDINIUM.
DR DrugBank; DB03270; 2,6-Difluorobenzenesulfonamide.
DR DrugBank; DB08083; 2-(1,3-thiazol-4-yl)-1H-benzimidazole-5-sulfonamide.
DR DrugBank; DB06954; 2-(cycloheptylmethyl)-1,1-dioxido-1-benzothiophen-6-yl sulfamate.
DR DrugBank; DB08659; 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide.
DR DrugBank; DB08046; 2-chloro-5-[(1S)-1-hydroxy-3-oxo-2H-isoindol-1-yl]benzenesulfonamide.
DR DrugBank; DB02087; 3,5-Difluorobenzenesulfonamide.
DR DrugBank; DB08156; 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID.
DR DrugBank; DB04203; 3-Mercuri-4-Aminobenzenesulfonamide.
DR DrugBank; DB04394; 3-Nitro-4-(2-Oxo-Pyrrolidin-1-Yl)-Benzenesulfonamide.
DR DrugBank; DB08782; 4-(2-AMINOETHYL)BENZENESULFONAMIDE.
DR DrugBank; DB04549; 4-(Aminosulfonyl)-N-[(2,3,4-Trifluorophenyl)Methyl]-Benzamide.
DR DrugBank; DB02221; 4-(Aminosulfonyl)-N-[(2,4,6-Trifluorophenyl)Methyl]-Benzamide.
DR DrugBank; DB04180; 4-(Aminosulfonyl)-N-[(2,4-Difluorophenyl)Methyl]-Benzamide.
DR DrugBank; DB03039; 4-(Aminosulfonyl)-N-[(2,5-Difluorophenyl)Methyl]-Benzamide.
DR DrugBank; DB02861; 4-(Aminosulfonyl)-N-[(3,4,5-Trifluorophenyl)Methyl]-Benzamide.
DR DrugBank; DB02429; 4-(Aminosulfonyl)-N-[(4-Fluorophenyl)Methyl]-Benzamide.
DR DrugBank; DB08202; 4-({[(4-METHYLPIPERAZIN-1-YL)AMINO]CARBONOTHIOYL}AMINO)BENZENESULFONAMIDE.
DR DrugBank; DB04600; 4-[(3-BROMO-4-O-SULFAMOYLBENZYL)(4-CYANOPHENYL)AMINO]-4H-[1,2,4]-TRIAZOLE.
DR DrugBank; DB04601; 4-[(4-O-SULFAMOYLBENZYL)(4-CYANOPHENYL)AMINO]-4H-[1,2,4]-TRIAZOLE.
DR DrugBank; DB01784; 4-Flourobenzenesulfonamide.
DR DrugBank; DB03385; 4-Methylimidazole.
DR DrugBank; DB03697; 4-Sulfonamide-[1-(4-Aminobutane)]Benzamide.
DR DrugBank; DB04002; 4-Sulfonamide-[4-(Thiomethylaminobutane)]Benzamide.
DR DrugBank; DB07632; 5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide.
DR DrugBank; DB07050; 5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide.
DR DrugBank; DB06891; 5-{[(4-AMINO-3-CHLORO-5-FLUOROPHENYL)SULFONYL]AMINO}-1,3,4-THIADIAZOLE-2-SULFONAMIDE.
DR DrugBank; DB08645; 6-CHLORO-3-(DICHLOROMETHYL)-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE-7-SULFONAMIDE 1,1-DIOXIDE.
DR DrugBank; DB08765; 6-HYDROXY-1,3-BENZOTHIAZOLE-2-SULFONAMIDE.
DR DrugBank; DB00819; Acetazolamide.
DR DrugBank; DB03877; AL-4623.
DR DrugBank; DB03262; Al-6619, [2h-Thieno[3,2-E]-1,2-Thiazine-6-Sulfonamide,2-(3-Hydroxyphenyl)-3-(4-Morpholinyl)-, 1,1-Dioxide].
DR DrugBank; DB03598; Al-6629, [2h-Thieno[3,2-E]-1,2-Thiazine-6-Sulfonamide,2-(3-Methoxyphenyl)-3-(4-Morpholinyl)-, 1,1-Dioxide].
DR DrugBank; DB04089; AL5300.
DR DrugBank; DB01964; AL5424.
DR DrugBank; DB03526; AL5927.
DR DrugBank; DB04371; AL6528.
DR DrugBank; DB02220; AL7089A.
DR DrugBank; DB03221; AL7099A.
DR DrugBank; DB02602; AL7182.
DR DrugBank; DB02535; Aminodi(Ethyloxy)Ethylaminocarbonylbenzenesulfonamide.
DR DrugBank; DB00436; Bendroflumethiazide.
DR DrugBank; DB00562; Benzthiazide.
DR DrugBank; DB01194; Brinzolamide.
DR DrugBank; DB00482; Celecoxib.
DR DrugBank; DB00880; Chlorothiazide.
DR DrugBank; DB02679; Cyanamide.
DR DrugBank; DB00606; Cyclothiazide.
DR DrugBank; DB02866; Dansylamide.
DR DrugBank; DB01119; Diazoxide.
DR DrugBank; DB01144; Diclofenamide.
DR DrugBank; DB00869; Dorzolamide.
DR DrugBank; DB08846; Ellagic acid.
DR DrugBank; DB01031; Ethinamate.
DR DrugBank; DB00311; Ethoxzolamide.
DR DrugBank; DB08157; ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB00695; Furosemide.
DR DrugBank; DB00774; Hydroflumethiazide.
DR DrugBank; DB08165; indane-5-sulfonamide.
DR DrugBank; DB02292; Irosustat.
DR DrugBank; DB03975; Mercuribenzoic Acid.
DR DrugBank; DB00703; Methazolamide.
DR DrugBank; DB00232; Methyclothiazide.
DR DrugBank; DB02610; N-(2,3,4,5,6-Pentaflouro-Benzyl)-4-Sulfamoyl-Benzamide.
DR DrugBank; DB07742; N-(2,3-DIFLUORO-BENZYL)-4-SULFAMOYL-BENZAMIDE.
DR DrugBank; DB03844; N-(2,6-Diflouro-Benzyl)-4-Sulfamoyl-Benzamide.
DR DrugBank; DB02069; N-(2-Flouro-Benzyl)-4-Sulfamoyl-Benzamide.
DR DrugBank; DB02986; N-(2-Thienylmethyl)-2,5-Thiophenedisulfonamide.
DR DrugBank; DB08301; N-({[4-(AMINOSULFONYL)PHENYL]AMINO}CARBONYL)-4-METHYLBENZENESULFONAMIDE.
DR DrugBank; DB07048; N-[(2R)-5-(aminosulfonyl)-2,3-dihydro-1H-inden-2-yl]-2-propylpentanamide.
DR DrugBank; DB03596; N-[2-(1h-Indol-5-Yl)-Butyl]-4-Sulfamoyl-Benzamide.
DR DrugBank; DB07476; N-[4-(AMINOSULFONYL)PHENYL]-2-MERCAPTOBENZAMIDE.
DR DrugBank; DB01748; N-Benzyl-4-Sulfamoyl-Benzamide.
DR DrugBank; DB08155; N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE.
DR DrugBank; DB01671; p-Hydroxymercuribenzoic acid.
DR DrugBank; DB07710; PHENYLALANYLAMINODI(ETHYLOXY)ETHYL BENZENESULFONAMIDEAMINOCARBONYLBENZENESULFONAMIDE.
DR DrugBank; DB01325; Quinethazone.
DR DrugBank; DB09460; Sodium carbonate.
DR DrugBank; DB09472; Sodium sulfate.
DR DrugBank; DB02894; Sulfamic Acid 2,3-O-(1-Methylethylidene)-4,5-O-Sulfonyl-Beta-Fructopyranose Ester.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB08329; Sulthiame.
DR DrugBank; DB07363; THIOPHENE-2,5-DISULFONIC ACID 2-AMIDE-5-(4-METHYL-BENZYLAMIDE).
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB01021; Trichlormethiazide.
DR DrugBank; DB03904; Urea.
DR DrugBank; DB00580; Valdecoxib.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; P00918; -.
DR GuidetoPHARMACOLOGY; 3092; -.
DR GlyGen; P00918; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P00918; -.
DR PhosphoSitePlus; P00918; -.
DR BioMuta; CA2; -.
DR OGP; P00918; -.
DR REPRODUCTION-2DPAGE; IPI00218414; -.
DR REPRODUCTION-2DPAGE; P00918; -.
DR UCD-2DPAGE; P00918; -.
DR CPTAC; CPTAC-177; -.
DR CPTAC; CPTAC-178; -.
DR EPD; P00918; -.
DR jPOST; P00918; -.
DR MassIVE; P00918; -.
DR PaxDb; P00918; -.
DR PeptideAtlas; P00918; -.
DR PRIDE; P00918; -.
DR ProteomicsDB; 51292; -.
DR Antibodypedia; 677; 689 antibodies from 42 providers.
DR DNASU; 760; -.
DR Ensembl; ENST00000285379.10; ENSP00000285379.4; ENSG00000104267.10.
DR GeneID; 760; -.
DR KEGG; hsa:760; -.
DR MANE-Select; ENST00000285379.10; ENSP00000285379.4; NM_000067.3; NP_000058.1.
DR CTD; 760; -.
DR DisGeNET; 760; -.
DR GeneCards; CA2; -.
DR HGNC; HGNC:1373; CA2.
DR HPA; ENSG00000104267; Tissue enhanced (intestine, stomach).
DR MalaCards; CA2; -.
DR MIM; 259730; phenotype.
DR MIM; 611492; gene.
DR neXtProt; NX_P00918; -.
DR OpenTargets; ENSG00000104267; -.
DR Orphanet; 2785; Osteopetrosis with renal tubular acidosis.
DR PharmGKB; PA25989; -.
DR VEuPathDB; HostDB:ENSG00000104267; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160385; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P00918; -.
DR OMA; SADFPNF; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P00918; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 2681.
DR PathwayCommons; P00918; -.
DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR SABIO-RK; P00918; -.
DR SignaLink; P00918; -.
DR BioGRID-ORCS; 760; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; CA2; human.
DR EvolutionaryTrace; P00918; -.
DR GeneWiki; Carbonic_anhydrase_II; -.
DR GenomeRNAi; 760; -.
DR Pharos; P00918; Tclin.
DR PRO; PR:P00918; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P00918; protein.
DR Bgee; ENSG00000104267; Expressed in colonic mucosa and 189 other tissues.
DR ExpressionAtlas; P00918; baseline and differential.
DR Genevisible; P00918; HS.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004064; F:arylesterase activity; IMP:CACAO.
DR GO; GO:0004089; F:carbonate dehydratase activity; IMP:CACAO.
DR GO; GO:0018820; F:cyanamide hydratase activity; IEA:RHEA.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IBA:GO_Central.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0032849; P:positive regulation of cellular pH reduction; IEA:Ensembl.
DR GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0044070; P:regulation of anion transport; IDA:UniProtKB.
DR GO; GO:2001225; P:regulation of chloride transport; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
DR GO; GO:0046903; P:secretion; IEA:Ensembl.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Disease variant; Lyase; Membrane; Metal-binding;
KW Osteopetrosis; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4207120,
FT ECO:0000269|PubMed:823150"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077418"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 64
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:15667203,
FT ECO:0000305|PubMed:17330962"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11076507,
FT ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
FT ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
FT ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
FT ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826,
FT ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386,
FT ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
FT ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673,
FT ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430,
FT ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389,
FT ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974,
FT ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11076507,
FT ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
FT ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
FT ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
FT ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440,
FT ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850,
FT ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987,
FT ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159,
FT ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242,
FT ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494,
FT ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308,
FT ECO:0000269|PubMed:9865942"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11076507,
FT ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
FT ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
FT ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
FT ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440,
FT ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850,
FT ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987,
FT ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159,
FT ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242,
FT ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494,
FT ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308,
FT ECO:0000269|PubMed:9865942"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10550681,
FT ECO:0000269|PubMed:19520834"
FT SITE 7
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000305|PubMed:17330962"
FT SITE 62
FT /note="Fine-tunes the proton-transfer properties of H-64;
FT involved in the binding of some activators, including
FT histamine and L-histidine"
FT /evidence="ECO:0000269|PubMed:16214338,
FT ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962"
FT SITE 67
FT /note="Fine-tunes the proton-transfer properties of H-64;
FT involved in the binding of some activators, including
FT histamine and L-histidine"
FT /evidence="ECO:0000269|PubMed:16214338,
FT ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962"
FT SITE 92
FT /note="Involved in the binding of some activators,
FT including histamine and L-histidine"
FT /evidence="ECO:0000269|PubMed:16214338,
FT ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4207120,
FT ECO:0000269|PubMed:823150"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27139"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 18
FT /note="K -> E (in Jogjakarta; dbSNP:rs118203931)"
FT /evidence="ECO:0000269|PubMed:6817747"
FT /id="VAR_001380"
FT VARIANT 92
FT /note="Q -> P (in OPTB3; in Czechoslovakia;
FT dbSNP:rs1304160279)"
FT /evidence="ECO:0000269|PubMed:15300855,
FT ECO:0000269|PubMed:9143915"
FT /id="VAR_001381"
FT VARIANT 94
FT /note="H -> Y (in OPTB3; partial loss of activity)"
FT /evidence="ECO:0000269|PubMed:15300855"
FT /id="VAR_021009"
FT VARIANT 107
FT /note="H -> Y (in OPTB3; dbSNP:rs118203933)"
FT /evidence="ECO:0000269|PubMed:15300855,
FT ECO:0000269|PubMed:1542674, ECO:0000269|PubMed:1928091,
FT ECO:0000269|PubMed:8834238"
FT /id="VAR_001382"
FT VARIANT 144
FT /note="G -> R (in OPTB3; complete loss of activity)"
FT /evidence="ECO:0000269|PubMed:15300855"
FT /id="VAR_021010"
FT VARIANT 236
FT /note="P -> H (in Melbourne; dbSNP:rs118203932)"
FT /evidence="ECO:0000269|PubMed:6407977"
FT /id="VAR_001383"
FT VARIANT 252
FT /note="N -> D (in dbSNP:rs2228063)"
FT /id="VAR_001384"
FT MUTAGEN 5
FT /note="W->A: Impaired activity, not rescued by 4-
FT methylimidazole (4-MI); when associated with W-64."
FT /evidence="ECO:0000269|PubMed:17071654"
FT MUTAGEN 7
FT /note="Y->F: Enhanced activity."
FT /evidence="ECO:0000269|PubMed:12171926,
FT ECO:0000269|PubMed:17330962"
FT MUTAGEN 7
FT /note="Y->H: Reduced proton transfer rate."
FT /evidence="ECO:0000269|PubMed:12171926,
FT ECO:0000269|PubMed:17330962"
FT MUTAGEN 62
FT /note="N->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18942852"
FT MUTAGEN 62
FT /note="N->D: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:18942852"
FT MUTAGEN 62
FT /note="N->H: Reduced proton transfer; when associated with
FT A-64."
FT /evidence="ECO:0000269|PubMed:15667203,
FT ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852"
FT MUTAGEN 62
FT /note="N->L: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17330962,
FT ECO:0000269|PubMed:18942852"
FT MUTAGEN 62
FT /note="N->T: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18942852"
FT MUTAGEN 62
FT /note="N->V: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18942852"
FT MUTAGEN 64
FT /note="H->A: Reduced CO(2) hydrase activity, rescued by 4-
FT methylimidazole (4-MI). Reduced proton transfer; when
FT associated with H-62. Enhanced proton transfer; when
FT associated with H-67. Enhanced proton transfer capacity;
FT when associated with H-99."
FT /evidence="ECO:0000269|PubMed:11327835,
FT ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:16106378,
FT ECO:0000269|PubMed:17071654"
FT MUTAGEN 64
FT /note="H->G: Impaired activity, not rescued by 4-
FT methylimidazole (4-MI)."
FT /evidence="ECO:0000269|PubMed:11327835,
FT ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"
FT MUTAGEN 64
FT /note="H->W: Impaired activity, rescued by 4-
FT methylimidazole (4-MI). Impaired activity, not rescued by
FT 4-methylimidazole (4-MI); when associated with A-5."
FT /evidence="ECO:0000269|PubMed:11327835,
FT ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"
FT MUTAGEN 65
FT /note="A->F: Reduced activity."
FT MUTAGEN 65
FT /note="A->S: 2-fold decrease in enzyme efficiency, as
FT determined by kcat/KM ratio, and efficiently inhibited by
FT chlorzolamide; when associated with Q-67."
FT /evidence="ECO:0000269|PubMed:19170619"
FT MUTAGEN 67
FT /note="N->H: Enhanced proton transfer; when associated with
FT A-64."
FT /evidence="ECO:0000269|PubMed:15667203"
FT MUTAGEN 67
FT /note="N->L: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17330962"
FT MUTAGEN 67
FT /note="N->Q: 2-fold decrease in enzyme efficiency, as
FT determined by kcat/KM ratio, and efficiently inhibited by
FT chlorzolamide; when associated with S-65."
FT /evidence="ECO:0000269|PubMed:19170619"
FT MUTAGEN 94
FT /note="H->C,D,E,N,Q: Strongly reduced CO(2) hydrase and p-
FT nitrophenyl acetate esterase activities, impaired stability
FT of zinc binding."
FT /evidence="ECO:0000269|PubMed:8431430,
FT ECO:0000269|PubMed:9398308"
FT MUTAGEN 106
FT /note="E->A,Q: Strongly reduced CO(2) hydrase activity."
FT /evidence="ECO:0000269|PubMed:15299482,
FT ECO:0000269|PubMed:7901850"
FT MUTAGEN 106
FT /note="E->D: Normal CO(2) hydrase activity."
FT /evidence="ECO:0000269|PubMed:15299482,
FT ECO:0000269|PubMed:7901850"
FT MUTAGEN 117
FT /note="E->Q: Strongly reduced activity and sulfonamide
FT affinity."
FT /evidence="ECO:0000269|PubMed:8639494"
FT MUTAGEN 119
FT /note="H->D,N,Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:9398308"
FT MUTAGEN 119
FT /note="H->E: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:9398308"
FT MUTAGEN 121
FT /note="V->A,G,I,L,S: Reduced CO(2) hydrase and p-
FT nitrophenyl acetate esterase activities."
FT /evidence="ECO:0000269|PubMed:1910042"
FT MUTAGEN 121
FT /note="V->K,R: Strongly reduced CO(2) hydrase and p-
FT nitrophenyl acetate esterase activities."
FT /evidence="ECO:0000269|PubMed:1910042"
FT MUTAGEN 142
FT /note="V->F,Y: Strongly impaired activity."
FT /evidence="ECO:0000269|PubMed:1932029"
FT MUTAGEN 142
FT /note="V->G: Weakly impaired activity."
FT /evidence="ECO:0000269|PubMed:1932029"
FT MUTAGEN 142
FT /note="V->H: Impaired activity."
FT /evidence="ECO:0000269|PubMed:1932029"
FT MUTAGEN 197
FT /note="L->A: Reduced CO(2) hydrase activity."
FT /evidence="ECO:0000269|PubMed:8485129"
FT MUTAGEN 197
FT /note="L->E,H,R: Strongly reduced CO(2) hydrase activity."
FT /evidence="ECO:0000269|PubMed:8485129"
FT MUTAGEN 197
FT /note="L->F: Normal activity."
FT /evidence="ECO:0000269|PubMed:8485129"
FT MUTAGEN 198
FT /note="T->A,C,H,P: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:12056894,
FT ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
FT ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"
FT MUTAGEN 198
FT /note="T->D,E: Strongly reduced activity, but enhanced zinc
FT affinity."
FT /evidence="ECO:0000269|PubMed:12056894,
FT ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
FT ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"
FT MUTAGEN 198
FT /note="T->S,V: Reduced activity."
FT /evidence="ECO:0000269|PubMed:12056894,
FT ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
FT ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"
FT MUTAGEN 199
FT /note="T->H: Higher affinity for bicarbonate. Enhanced
FT proton transfer capacity; when associated with A-64."
FT /evidence="ECO:0000269|PubMed:16106378,
FT ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:8451242"
FT MUTAGEN 199
FT /note="T->S: Enhanced p-nitrophenyl acetate esterase
FT activity, but normal CO(2) hydrase activity."
FT /evidence="ECO:0000269|PubMed:16106378,
FT ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:8451242"
FT MUTAGEN 201
FT /note="P->A: Normal CO(2) hydrase activity, but impaired
FT stability."
FT /evidence="ECO:0000269|PubMed:8218160"
FT CONFLICT 179..180
FT /note="DP -> AA (in Ref. 6; AAH11949)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5Y2R"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3K34"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2X7S"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3KS3"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3KOI"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3K34"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5GMN"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6Q9T"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6QEB"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3K34"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:3K34"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:4QK3"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3K34"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:7Q0C"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3K34"
SQ SEQUENCE 260 AA; 29246 MW; 2EC2BB7548F10558 CRC64;
MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL
NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL
VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP
RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM
VDNWRPAQPL KNRQIKASFK
