RL2_ECOLI
ID RL2_ECOLI Reviewed; 273 AA.
AC P60422; P02387; Q2M6Y2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=50S ribosomal protein L2;
DE AltName: Full=Large ribosomal subunit protein uL2 {ECO:0000303|PubMed:24524803};
GN Name=rplB; OrderedLocusNames=b3317, JW3279;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3892488; DOI=10.1093/nar/13.12.4521;
RA Zurawski G., Zurawski S.M.;
RT "Structure of the Escherichia coli S10 ribosomal protein operon.";
RL Nucleic Acids Res. 13:4521-4526(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-273, AND SUBUNIT.
RA Kimura M., Mende L., Wittmann-Liebold B.;
RT "The primary structure of protein L2 from the Escherichia coli ribosome.";
RL FEBS Lett. 149:304-312(1982).
RN [5]
RP PROTEIN SEQUENCE OF 60-71 AND 200-208, SUBUNIT, AND CROSS-LINKING TO RRNA.
RC STRAIN=MRE-600;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [6]
RP ASSEMBLY MAP OF THE 50S SUBUNIT.
RC STRAIN=K12;
RX PubMed=3298242; DOI=10.1016/s0021-9258(18)47489-3;
RA Herold M., Nierhaus K.H.;
RT "Incorporation of six additional proteins to complete the assembly map of
RT the 50 S subunit from Escherichia coli ribosomes.";
RL J. Biol. Chem. 262:8826-8833(1987).
RN [7]
RP MUTAGENESIS OF HIS-230.
RX PubMed=8722025; DOI=10.1139/o95-117;
RA Cooperman B.S., Wooten T., Romero D.P., Traut R.R.;
RT "Histidine 229 in protein L2 is apparently essential for 50S peptidyl
RT transferase activity.";
RL Biochem. Cell Biol. 73:1087-1094(1995).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP PROTEIN REPLACEMENT STUDIES.
RX PubMed=9531480; DOI=10.1042/bj3310423;
RA Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.;
RT "Functional implications of ribosomal protein L2 in protein biosynthesis as
RT shown by in vivo replacement studies.";
RL Biochem. J. 331:423-430(1998).
RN [10]
RP REQUIREMENT FOR 70S RIBOSOME FORMATION, TRNA-BINDING, AND MUTAGENESIS OF
RP CONSERVED RESIDUES.
RX PubMed=11013226; DOI=10.1093/emboj/19.19.5241;
RA Diedrich G., Spahn C.M.T., Stelzl U., Schaefer M.A., Wooten T.,
RA Bochkariov D.E., Cooperman B.S., Traut R.R., Nierhaus K.H.;
RT "Ribosomal protein L2 is involved in the association of the ribosomal
RT subunits, tRNA binding to A and P sites and peptidyl transfer.";
RL EMBO J. 19:5241-5250(2000).
RN [11]
RP POSITION IN THE 50S SUBUNIT AND 70S RIBOSOME, AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=11114255; DOI=10.1006/jmbi.2000.4289;
RA Willumeit R., Forthmann S., Beckmann J., Diedrich G., Ratering R.,
RA Stuhrmann H.B., Nierhaus K.H.;
RT "Localization of the protein L2 in the 50 S subunit and the 70 S E. coli
RT ribosome.";
RL J. Mol. Biol. 305:167-177(2001).
RN [12]
RP MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-242, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [14]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [15]
RP 3D-STRUCTURE MODELING, AND SUBUNIT.
RX PubMed=10756104; DOI=10.1006/jmbi.2000.3635;
RA Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J.,
RA Goerlach M., van Heel M., Brimacombe R.;
RT "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S
RT ribosomal subunit based on a cryo-electron microscopic reconstruction at
RT 7.5 A resolution.";
RL J. Mol. Biol. 298:35-59(2000).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), SUBUNIT, AND
RP INTERSUBUNIT BRIDGE FORMATION.
RC STRAIN=MRE-600;
RX PubMed=12809609; DOI=10.1016/s0092-8674(03)00427-6;
RA Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
RA Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using real-
RT space refinement.";
RL Cell 113:789-801(2003).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES,
RP AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A.,
RA Holton J.M., Cate J.H.D.;
RT "Structures of the bacterial ribosome at 3.5 A resolution.";
RL Science 310:827-834(2005).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 2-272 IN TNAC-STALLED
RP 50S RIBOSOMAL SUBUNIT, AND SUBUNIT.
RC STRAIN=K12 / A19 / KC6;
RX PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA Bischoff L., Berninghausen O., Beckmann R.;
RT "Molecular basis for the ribosome functioning as an L-tryptophan sensor.";
RL Cell Rep. 9:469-475(2014).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 2-273 OF 50S RIBOSOMAL
RP SUBUNIT IN COMPLEX WITH OBGE AND GMP-PNP, AND SUBUNIT.
RX PubMed=24844575; DOI=10.1371/journal.pbio.1001866;
RA Feng B., Mandava C.S., Guo Q., Wang J., Cao W., Li N., Zhang Y., Zhang Y.,
RA Wang Z., Wu J., Sanyal S., Lei J., Gao N.;
RT "Structural and functional insights into the mode of action of a
RT universally conserved Obg GTPase.";
RL PLoS Biol. 12:E1001866-E1001866(2014).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906160; DOI=10.1038/nature20822;
RA Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT "Mechanistic insights into the alternative translation termination by ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT lacking stop codons.";
RL Nature 541:546-549(2017).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27934701; DOI=10.1126/science.aai9127;
RA James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT "Translational termination without a stop codon.";
RL Science 354:1437-1440(2016).
RN [23]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=28077875; DOI=10.1038/nature21053;
RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA Jin H.;
RT "Structural basis of co-translational quality control by ArfA and RF2 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: One of the primary rRNA binding proteins (PubMed:3298242).
CC Located near the base of the L1 stalk, it is probably also mobile.
CC Required for association of the 30S and 50S subunits to form the 70S
CC ribosome, for tRNA binding and peptide bond formation (PubMed:8722025).
CC It has been suggested to have peptidyltransferase activity; this is
CC highly controversial. {ECO:0000269|PubMed:10756104,
CC ECO:0000269|PubMed:11013226, ECO:0000269|PubMed:11114255,
CC ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117,
CC ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:8722025}.
CC -!- FUNCTION: In the E.coli 70S ribosome in the initiation state it has
CC been modeled to make several contacts with the 16S rRNA (forming bridge
CC B7b, PubMed:12809609); these contacts are broken in the model with
CC bound EF-G. {ECO:0000269|PubMed:12809609}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (Ref.4, PubMed:7556101,
CC PubMed:11114255, PubMed:10094780, PubMed:10756104, PubMed:12809609,
CC PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701,
CC PubMed:27906160, PubMed:27906161). Forms a bridge to the 30S subunit in
CC the 70S ribosome, contacting the 16S rRNA (PubMed:12809609). Interacts
CC weakly with S6 in one of the 3.5 A resolved structures.
CC {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:10756104,
CC ECO:0000269|PubMed:11114255, ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:24844575,
CC ECO:0000269|PubMed:25310980, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:7556101, ECO:0000269|Ref.4}.
CC -!- INTERACTION:
CC P60422; P03004: dnaA; NbExp=5; IntAct=EBI-543515, EBI-548951;
CC P60422; P45759: gspE; NbExp=2; IntAct=EBI-543515, EBI-1132437;
CC P60422; P00959: metG; NbExp=2; IntAct=EBI-543515, EBI-909268;
CC P60422; P0A7Z4: rpoA; NbExp=6; IntAct=EBI-543515, EBI-544985;
CC -!- MASS SPECTROMETRY: Mass=29732.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: This protein can be partially replaced in vivo by its
CC H.marismortui (HmaL2) or human (L8, from the 60S cytoplasmic ribosome)
CC homolog. {ECO:0000269|PubMed:9531480}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; X02613; CAA26463.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58114.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76342.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77974.1; -; Genomic_DNA.
DR PIR; E23129; R5EC2.
DR RefSeq; NP_417776.1; NC_000913.3.
DR RefSeq; WP_000301864.1; NZ_STEB01000038.1.
DR PDB; 2J28; EM; 8.00 A; C=4-270.
DR PDB; 2RDO; EM; 9.10 A; C=2-273.
DR PDB; 3BBX; EM; 10.00 A; C=1-273.
DR PDB; 3J5L; EM; 6.60 A; C=2-272.
DR PDB; 3J7Z; EM; 3.90 A; C=1-273.
DR PDB; 3J8G; EM; 5.00 A; C=1-273.
DR PDB; 3J9Y; EM; 3.90 A; C=1-273.
DR PDB; 3J9Z; EM; 3.60 A; LN=2-273.
DR PDB; 3JA1; EM; 3.60 A; LD=2-273.
DR PDB; 3JBU; EM; 3.64 A; c=1-273.
DR PDB; 3JBV; EM; 3.32 A; c=1-273.
DR PDB; 3JCD; EM; 3.70 A; C=1-273.
DR PDB; 3JCE; EM; 3.20 A; C=1-273.
DR PDB; 3JCJ; EM; 3.70 A; B=1-273.
DR PDB; 3JCN; EM; 4.60 A; C=1-273.
DR PDB; 487D; EM; 7.50 A; I=62-172.
DR PDB; 4CSU; EM; 5.50 A; C=2-273.
DR PDB; 4U1U; X-ray; 2.95 A; BC/DC=2-272.
DR PDB; 4U1V; X-ray; 3.00 A; BC/DC=2-272.
DR PDB; 4U20; X-ray; 2.90 A; BC/DC=2-272.
DR PDB; 4U24; X-ray; 2.90 A; BC/DC=2-272.
DR PDB; 4U25; X-ray; 2.90 A; BC/DC=2-272.
DR PDB; 4U26; X-ray; 2.80 A; BC/DC=2-272.
DR PDB; 4U27; X-ray; 2.80 A; BC/DC=2-272.
DR PDB; 4UY8; EM; 3.80 A; C=2-272.
DR PDB; 4V47; EM; 12.30 A; AA=2-273.
DR PDB; 4V48; EM; 11.50 A; AA=2-273.
DR PDB; 4V4H; X-ray; 3.46 A; BC/DC=1-273.
DR PDB; 4V4Q; X-ray; 3.46 A; BC/DC=1-273.
DR PDB; 4V4V; EM; 15.00 A; BA=39-265.
DR PDB; 4V4W; EM; 15.00 A; BA=39-265.
DR PDB; 4V50; X-ray; 3.22 A; BC/DC=2-273.
DR PDB; 4V52; X-ray; 3.21 A; BC/DC=2-273.
DR PDB; 4V53; X-ray; 3.54 A; BC/DC=2-273.
DR PDB; 4V54; X-ray; 3.30 A; BC/DC=2-273.
DR PDB; 4V55; X-ray; 4.00 A; BC/DC=2-273.
DR PDB; 4V56; X-ray; 3.93 A; BC/DC=2-273.
DR PDB; 4V57; X-ray; 3.50 A; BC/DC=2-273.
DR PDB; 4V5B; X-ray; 3.74 A; AC/CC=1-273.
DR PDB; 4V5H; EM; 5.80 A; BC=2-272.
DR PDB; 4V5Y; X-ray; 4.45 A; BC/DC=2-273.
DR PDB; 4V64; X-ray; 3.50 A; BC/DC=1-273.
DR PDB; 4V65; EM; 9.00 A; BN=1-270.
DR PDB; 4V66; EM; 9.00 A; BN=1-270.
DR PDB; 4V69; EM; 6.70 A; BC=2-272.
DR PDB; 4V6C; X-ray; 3.19 A; BC/DC=1-273.
DR PDB; 4V6D; X-ray; 3.81 A; BC/DC=1-273.
DR PDB; 4V6E; X-ray; 3.71 A; BC/DC=1-273.
DR PDB; 4V6K; EM; 8.25 A; AD=1-273.
DR PDB; 4V6L; EM; 13.20 A; BD=1-273.
DR PDB; 4V6M; EM; 7.10 A; B6=2-273.
DR PDB; 4V6N; EM; 12.10 A; AD=2-273.
DR PDB; 4V6O; EM; 14.70 A; BD=2-273.
DR PDB; 4V6P; EM; 13.50 A; BD=2-273.
DR PDB; 4V6Q; EM; 11.50 A; BD=2-273.
DR PDB; 4V6R; EM; 11.50 A; BD=2-273.
DR PDB; 4V6S; EM; 13.10 A; AD=2-273.
DR PDB; 4V6T; EM; 8.30 A; BC=2-272.
DR PDB; 4V6V; EM; 9.80 A; BD=2-273.
DR PDB; 4V6Y; EM; 12.00 A; BC=1-272.
DR PDB; 4V6Z; EM; 12.00 A; BC=1-272.
DR PDB; 4V70; EM; 17.00 A; BC=1-272.
DR PDB; 4V71; EM; 20.00 A; BC=1-272.
DR PDB; 4V72; EM; 13.00 A; BC=1-272.
DR PDB; 4V73; EM; 15.00 A; BC=1-272.
DR PDB; 4V74; EM; 17.00 A; BC=1-272.
DR PDB; 4V75; EM; 12.00 A; BC=1-272.
DR PDB; 4V76; EM; 17.00 A; BC=1-272.
DR PDB; 4V77; EM; 17.00 A; BC=1-272.
DR PDB; 4V78; EM; 20.00 A; BC=1-272.
DR PDB; 4V79; EM; 15.00 A; BC=1-272.
DR PDB; 4V7A; EM; 9.00 A; BC=1-272.
DR PDB; 4V7B; EM; 6.80 A; BC=1-273.
DR PDB; 4V7C; EM; 7.60 A; BD=2-273.
DR PDB; 4V7D; EM; 7.60 A; AD=2-273.
DR PDB; 4V7I; EM; 9.60 A; A6=1-273.
DR PDB; 4V7S; X-ray; 3.25 A; BC/DC=2-272.
DR PDB; 4V7T; X-ray; 3.19 A; BC/DC=2-272.
DR PDB; 4V7U; X-ray; 3.10 A; BC/DC=2-272.
DR PDB; 4V7V; X-ray; 3.29 A; BC/DC=2-272.
DR PDB; 4V85; X-ray; 3.20 A; BC=1-273.
DR PDB; 4V89; X-ray; 3.70 A; BC=1-273.
DR PDB; 4V9C; X-ray; 3.30 A; BC/DC=1-273.
DR PDB; 4V9D; X-ray; 3.00 A; CC/DC=2-272.
DR PDB; 4V9O; X-ray; 2.90 A; AC/CC/EC/GC=1-273.
DR PDB; 4V9P; X-ray; 2.90 A; AC/CC/EC/GC=1-273.
DR PDB; 4WF1; X-ray; 3.09 A; BC/DC=2-272.
DR PDB; 4WOI; X-ray; 3.00 A; BC/CC=1-273.
DR PDB; 4WWW; X-ray; 3.10 A; RC/YC=2-272.
DR PDB; 4YBB; X-ray; 2.10 A; CC/DC=2-272.
DR PDB; 5ADY; EM; 4.50 A; C=1-273.
DR PDB; 5AFI; EM; 2.90 A; C=1-273.
DR PDB; 5AKA; EM; 5.70 A; C=1-273.
DR PDB; 5GAD; EM; 3.70 A; C=1-273.
DR PDB; 5GAE; EM; 3.33 A; C=1-273.
DR PDB; 5GAF; EM; 4.30 A; C=2-272.
DR PDB; 5GAG; EM; 3.80 A; C=1-273.
DR PDB; 5GAH; EM; 3.80 A; C=1-273.
DR PDB; 5H5U; EM; 3.00 A; C=2-273.
DR PDB; 5IQR; EM; 3.00 A; B=1-273.
DR PDB; 5IT8; X-ray; 3.12 A; CC/DC=2-272.
DR PDB; 5J5B; X-ray; 2.80 A; CC/DC=2-272.
DR PDB; 5J7L; X-ray; 3.00 A; CC/DC=2-272.
DR PDB; 5J88; X-ray; 3.32 A; CC/DC=2-273.
DR PDB; 5J8A; X-ray; 3.10 A; CC/DC=2-273.
DR PDB; 5J91; X-ray; 2.96 A; CC/DC=2-273.
DR PDB; 5JC9; X-ray; 3.03 A; CC/DC=2-272.
DR PDB; 5JTE; EM; 3.60 A; BC=1-273.
DR PDB; 5JU8; EM; 3.60 A; BC=1-273.
DR PDB; 5KCR; EM; 3.60 A; 1D=1-273.
DR PDB; 5KCS; EM; 3.90 A; 1D=1-273.
DR PDB; 5KPS; EM; 3.90 A; B=1-273.
DR PDB; 5KPV; EM; 4.10 A; A=1-273.
DR PDB; 5KPW; EM; 3.90 A; A=1-273.
DR PDB; 5KPX; EM; 3.90 A; A=1-273.
DR PDB; 5L3P; EM; 3.70 A; D=1-273.
DR PDB; 5LZA; EM; 3.60 A; C=2-272.
DR PDB; 5LZB; EM; 5.30 A; C=2-272.
DR PDB; 5LZC; EM; 4.80 A; C=2-272.
DR PDB; 5LZD; EM; 3.40 A; C=2-272.
DR PDB; 5LZE; EM; 3.50 A; C=2-272.
DR PDB; 5LZF; EM; 4.60 A; C=2-272.
DR PDB; 5MDV; EM; 2.97 A; B=1-273.
DR PDB; 5MDW; EM; 3.06 A; B=1-273.
DR PDB; 5MDY; EM; 3.35 A; B=1-273.
DR PDB; 5MDZ; EM; 3.10 A; B=1-273.
DR PDB; 5MGP; EM; 3.10 A; C=2-272.
DR PDB; 5NCO; EM; 4.80 A; C=2-272.
DR PDB; 5NP6; EM; 3.60 A; a=2-272.
DR PDB; 5NWY; EM; 2.93 A; P=1-273.
DR PDB; 5O2R; EM; 3.40 A; C=2-272.
DR PDB; 5U4I; EM; 3.50 A; C=1-273.
DR PDB; 5U9F; EM; 3.20 A; 04=1-273.
DR PDB; 5U9G; EM; 3.20 A; 04=1-273.
DR PDB; 5UYK; EM; 3.90 A; 04=2-272.
DR PDB; 5UYL; EM; 3.60 A; 04=2-272.
DR PDB; 5UYM; EM; 3.20 A; 04=2-272.
DR PDB; 5UYN; EM; 4.00 A; 04=2-272.
DR PDB; 5UYP; EM; 3.90 A; 04=2-272.
DR PDB; 5UYQ; EM; 3.80 A; 04=2-272.
DR PDB; 5WDT; EM; 3.00 A; C=2-272.
DR PDB; 5WE4; EM; 3.10 A; C=2-272.
DR PDB; 5WE6; EM; 3.40 A; C=2-272.
DR PDB; 5WFK; EM; 3.40 A; C=2-272.
DR PDB; 6BU8; EM; 3.50 A; 04=2-272.
DR PDB; 6BY1; X-ray; 3.94 A; CC/DC=2-272.
DR PDB; 6C4H; EM; 3.10 A; C=1-273.
DR PDB; 6ENF; EM; 3.20 A; C=2-272.
DR PDB; 6ENJ; EM; 3.70 A; C=2-272.
DR PDB; 6ENU; EM; 3.10 A; C=2-272.
DR PDB; 6GBZ; EM; 3.80 A; C=2-272.
DR PDB; 6GC0; EM; 3.80 A; C=2-272.
DR PDB; 6GC4; EM; 4.30 A; C=2-272.
DR PDB; 6GC6; EM; 4.30 A; C=2-224.
DR PDB; 6GC8; EM; 3.80 A; C=2-272.
DR PDB; 6GWT; EM; 3.80 A; C=2-272.
DR PDB; 6GXM; EM; 3.80 A; C=2-272.
DR PDB; 6GXN; EM; 3.90 A; C=2-272.
DR PDB; 6GXO; EM; 3.90 A; C=2-272.
DR PDB; 6GXP; EM; 4.40 A; C=2-272.
DR PDB; 6H4N; EM; 3.00 A; C=2-272.
DR PDB; 6H58; EM; 7.90 A; C/CC=2-272.
DR PDB; 6HRM; EM; 2.96 A; B=2-272.
DR PDB; 6I0Y; EM; 3.20 A; C=1-273.
DR PDB; 6I7V; X-ray; 2.90 A; CC/DC=2-272.
DR PDB; 6O9J; EM; 3.90 A; C=4-270.
DR PDB; 6O9K; EM; 4.00 A; 9=2-272.
DR PDB; 6OFX; EM; 3.30 A; b=2-272.
DR PDB; 6OG7; EM; 3.30 A; b=2-272.
DR PDB; 6OGF; EM; 3.90 A; b=1-273.
DR PDB; 6OGG; EM; 4.20 A; b=1-273.
DR PDB; 6OGI; EM; 3.40 A; b=1-273.
DR PDB; 6OM6; EM; 3.10 A; B=1-273.
DR PDB; 6ORE; EM; 2.90 A; B=2-272.
DR PDB; 6ORL; EM; 3.50 A; B=2-272.
DR PDB; 6OST; EM; 4.20 A; B=2-272.
DR PDB; 6OT3; EM; 3.90 A; B=2-272.
DR PDB; 6OUO; EM; 3.70 A; B=2-272.
DR PDB; 6PC5; EM; 2.70 A; K=2-272.
DR PDB; 6PC6; EM; 2.50 A; K=2-272.
DR PDB; 6PC7; EM; 2.50 A; K=2-272.
DR PDB; 6PC8; EM; 2.90 A; K=2-272.
DR PDB; 6PCH; EM; 2.90 A; K=2-272.
DR PDB; 6PCQ; EM; 2.60 A; K=2-272.
DR PDB; 6PCR; EM; 2.50 A; K=2-272.
DR PDB; 6PCS; EM; 2.80 A; K=2-272.
DR PDB; 6PCT; EM; 2.80 A; K=2-272.
DR PDB; 6Q98; EM; 4.30 A; B=1-273.
DR PDB; 6Q9A; EM; 3.70 A; B=2-272.
DR PDB; 6QDW; EM; 2.83 A; c=1-273.
DR PDB; 6QUL; EM; 3.00 A; C=1-273.
DR PDB; 6S0K; EM; 3.10 A; C=1-273.
DR PDB; 6SZS; EM; 3.06 A; C=1-273.
DR PDB; 6TBV; EM; 2.70 A; L021=1-273.
DR PDB; 6TC3; EM; 2.70 A; L021=1-273.
DR PDB; 6VU3; EM; 3.70 A; h=2-272.
DR PDB; 6VWL; EM; 3.10 A; A=1-273.
DR PDB; 6VWM; EM; 3.40 A; A=1-273.
DR PDB; 6VWN; EM; 3.40 A; A=1-273.
DR PDB; 6VYQ; EM; 3.70 A; h=1-273.
DR PDB; 6VYR; EM; 3.80 A; h=1-273.
DR PDB; 6VYS; EM; 3.70 A; h=1-273.
DR PDB; 6VYT; EM; 14.00 A; h=1-273.
DR PDB; 6VYU; EM; 7.00 A; h=1-273.
DR PDB; 6VYW; EM; 7.00 A; h=1-273.
DR PDB; 6VYX; EM; 9.90 A; h=1-273.
DR PDB; 6VYY; EM; 9.90 A; h=1-273.
DR PDB; 6VYZ; EM; 9.90 A; h=1-273.
DR PDB; 6VZ2; EM; 10.00 A; h=2-272.
DR PDB; 6VZ3; EM; 8.90 A; h=2-272.
DR PDB; 6VZ5; EM; 8.90 A; h=1-273.
DR PDB; 6VZ7; EM; 7.00 A; h=2-272.
DR PDB; 6VZJ; EM; 4.10 A; h=2-272.
DR PDB; 6WD0; EM; 3.00 A; b=2-272.
DR PDB; 6WD1; EM; 3.30 A; b=2-272.
DR PDB; 6WD2; EM; 3.60 A; b=2-272.
DR PDB; 6WD3; EM; 3.60 A; b=2-272.
DR PDB; 6WD4; EM; 3.70 A; b=2-272.
DR PDB; 6WD5; EM; 3.60 A; b=2-272.
DR PDB; 6WD6; EM; 3.70 A; b=2-272.
DR PDB; 6WD7; EM; 3.90 A; b=2-272.
DR PDB; 6WD8; EM; 3.70 A; b=2-272.
DR PDB; 6WD9; EM; 3.70 A; b=2-272.
DR PDB; 6WDA; EM; 3.80 A; b=2-272.
DR PDB; 6WDB; EM; 4.00 A; b=2-272.
DR PDB; 6WDC; EM; 4.20 A; b=2-272.
DR PDB; 6WDD; EM; 3.20 A; b=2-272.
DR PDB; 6WDE; EM; 3.00 A; b=2-272.
DR PDB; 6WDF; EM; 3.30 A; b=2-272.
DR PDB; 6WDG; EM; 3.30 A; b=2-272.
DR PDB; 6WDH; EM; 4.30 A; b=2-272.
DR PDB; 6WDI; EM; 4.00 A; b=2-272.
DR PDB; 6WDJ; EM; 3.70 A; b=2-272.
DR PDB; 6WDK; EM; 3.60 A; b=2-272.
DR PDB; 6WDL; EM; 3.70 A; b=2-272.
DR PDB; 6WDM; EM; 3.60 A; b=2-272.
DR PDB; 6WNT; EM; 3.10 A; b=2-272.
DR PDB; 6WNV; EM; 3.50 A; b=2-272.
DR PDB; 6WNW; EM; 3.20 A; b=2-272.
DR PDB; 6WYV; EM; 2.75 A; K=2-272.
DR PDB; 6X6T; EM; 3.20 A; h=1-273.
DR PDB; 6X7F; EM; 3.50 A; h=1-273.
DR PDB; 6X7K; EM; 3.10 A; h=1-273.
DR PDB; 6X9Q; EM; 4.80 A; h=1-273.
DR PDB; 6XDQ; EM; 3.70 A; h=1-273.
DR PDB; 6XDR; EM; 4.70 A; h=1-273.
DR PDB; 6XGF; EM; 5.00 A; h=1-273.
DR PDB; 6XII; EM; 7.00 A; h=1-273.
DR PDB; 6XIJ; EM; 8.00 A; h=1-273.
DR PDB; 6XZ7; EM; 2.10 A; C=2-272.
DR PDB; 6XZA; EM; 2.66 A; C2=2-272.
DR PDB; 6XZB; EM; 2.54 A; C2=2-272.
DR PDB; 6Y69; EM; 2.86 A; C=2-272.
DR PDB; 6YS3; EM; 2.58 A; c=1-273.
DR PDB; 6YSR; EM; 3.10 A; C=1-273.
DR PDB; 6YSS; EM; 2.60 A; C=1-273.
DR PDB; 6YST; EM; 3.20 A; C=1-273.
DR PDB; 6YSU; EM; 3.70 A; C=1-273.
DR PDB; 6ZTJ; EM; 3.40 A; BC=1-273.
DR PDB; 6ZTL; EM; 3.50 A; BC=1-273.
DR PDB; 6ZTM; EM; 3.30 A; BC=1-273.
DR PDB; 6ZTN; EM; 3.90 A; BC=1-273.
DR PDB; 6ZTO; EM; 3.00 A; BC=1-273.
DR PDB; 6ZTP; EM; 3.00 A; BC=1-273.
DR PDB; 6ZU1; EM; 3.00 A; BC=1-273.
DR PDB; 7ABZ; EM; 3.21 A; B=2-272.
DR PDB; 7AC7; EM; 3.08 A; B=2-272.
DR PDB; 7ACJ; EM; 3.20 A; B=2-272.
DR PDB; 7ACR; EM; 3.44 A; B=2-272.
DR PDB; 7B5K; EM; 2.90 A; C=2-272.
DR PDB; 7BL2; EM; 3.70 A; C=1-273.
DR PDB; 7BL3; EM; 3.50 A; C=1-273.
DR PDB; 7BL4; EM; 2.40 A; C=1-273.
DR PDB; 7BL5; EM; 3.30 A; C=1-273.
DR PDB; 7BL6; EM; 4.00 A; C=1-273.
DR PDB; 7BV8; EM; 3.14 A; C=1-273.
DR PDB; 7D6Z; EM; 3.40 A; C=1-273.
DR PDB; 7D80; EM; 4.10 A; b=1-273.
DR PDB; 7JSS; EM; 3.70 A; b=2-272.
DR PDB; 7JSW; EM; 3.80 A; b=2-272.
DR PDB; 7JSZ; EM; 3.70 A; b=2-272.
DR PDB; 7JT1; EM; 3.30 A; b=2-272.
DR PDB; 7JT2; EM; 3.50 A; b=2-272.
DR PDB; 7JT3; EM; 3.70 A; b=2-272.
DR PDB; 7K00; EM; 1.98 A; c=1-273.
DR PDB; 7K50; EM; 3.40 A; b=2-272.
DR PDB; 7K51; EM; 3.50 A; b=2-272.
DR PDB; 7K52; EM; 3.40 A; b=2-272.
DR PDB; 7K53; EM; 3.20 A; b=2-272.
DR PDB; 7K54; EM; 3.20 A; b=2-272.
DR PDB; 7K55; EM; 3.30 A; b=2-272.
DR PDB; 7LV0; EM; 3.20 A; b=2-272.
DR PDB; 7LVK; EM; 2.20 A; K=1-273.
DR PDB; 7N1P; EM; 2.33 A; LB=1-273.
DR PDB; 7N2C; EM; 2.72 A; LB=1-273.
DR PDB; 7N2U; EM; 2.53 A; LB=1-273.
DR PDB; 7N2V; EM; 2.54 A; LB=1-273.
DR PDB; 7N30; EM; 2.66 A; LB=1-273.
DR PDB; 7N31; EM; 2.69 A; LB=1-273.
DR PDB; 7NBU; EM; 3.11 A; c=2-272.
DR PDB; 7NSO; EM; 2.90 A; C=2-272.
DR PDB; 7NSP; EM; 3.50 A; C=2-272.
DR PDB; 7NSQ; EM; 3.10 A; C=2-272.
DR PDB; 7NWT; EM; 2.66 A; B=1-273.
DR PDB; 7NWW; EM; 3.05 A; C=2-272.
DR PDB; 7O19; EM; 2.90 A; BC=1-273.
DR PDB; 7O1A; EM; 2.40 A; BC=1-273.
DR PDB; 7O1C; EM; 2.60 A; BC=1-273.
DR PDB; 7OIF; EM; 3.00 A; C=2-272.
DR PDB; 7OIG; EM; 3.20 A; C=2-272.
DR PDB; 7OII; EM; 3.00 A; C=2-272.
DR PDB; 7OIZ; EM; 2.90 A; c=1-273.
DR PDB; 7OJ0; EM; 3.50 A; c=1-273.
DR PDB; 7OT5; EM; 2.90 A; C=2-272.
DR PDB; 7P3K; EM; 2.90 A; c=1-273.
DR PDB; 7PJS; EM; 2.35 A; C=1-273.
DR PDB; 7PJT; EM; 6.00 A; C=1-273.
DR PDB; 7PJV; EM; 3.10 A; C=1-273.
DR PDB; 7PJW; EM; 4.00 A; C=1-273.
DR PDB; 7PJX; EM; 6.50 A; C=1-273.
DR PDB; 7PJY; EM; 3.10 A; C=1-273.
DR PDB; 7PJZ; EM; 6.00 A; C=1-273.
DR PDB; 7QG8; EM; 3.97 A; P=1-273.
DR PDB; 7S1G; EM; 2.48 A; K=1-273.
DR PDB; 7S1H; EM; 2.35 A; K=1-273.
DR PDB; 7S1I; EM; 2.48 A; K=1-273.
DR PDB; 7S1J; EM; 2.47 A; K=1-273.
DR PDB; 7S1K; EM; 2.42 A; K=1-273.
DR PDB; 7SS9; EM; 3.90 A; b=2-272.
DR PDB; 7SSD; EM; 3.30 A; b=2-272.
DR PDB; 7SSL; EM; 3.80 A; b=2-272.
DR PDB; 7SSN; EM; 3.20 A; b=2-272.
DR PDB; 7SSO; EM; 3.20 A; b=2-272.
DR PDB; 7SSW; EM; 3.80 A; b=2-272.
DR PDB; 7ST2; EM; 2.90 A; b=2-272.
DR PDB; 7ST6; EM; 3.00 A; b=2-272.
DR PDB; 7ST7; EM; 3.20 A; b=2-272.
DR PDBsum; 2J28; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3BBX; -.
DR PDBsum; 3J5L; -.
DR PDBsum; 3J7Z; -.
DR PDBsum; 3J8G; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JBU; -.
DR PDBsum; 3JBV; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 3JCN; -.
DR PDBsum; 487D; -.
DR PDBsum; 4CSU; -.
DR PDBsum; 4U1U; -.
DR PDBsum; 4U1V; -.
DR PDBsum; 4U20; -.
DR PDBsum; 4U24; -.
DR PDBsum; 4U25; -.
DR PDBsum; 4U26; -.
DR PDBsum; 4U27; -.
DR PDBsum; 4UY8; -.
DR PDBsum; 4V47; -.
DR PDBsum; 4V48; -.
DR PDBsum; 4V4H; -.
DR PDBsum; 4V4Q; -.
DR PDBsum; 4V4V; -.
DR PDBsum; 4V4W; -.
DR PDBsum; 4V50; -.
DR PDBsum; 4V52; -.
DR PDBsum; 4V53; -.
DR PDBsum; 4V54; -.
DR PDBsum; 4V55; -.
DR PDBsum; 4V56; -.
DR PDBsum; 4V57; -.
DR PDBsum; 4V5B; -.
DR PDBsum; 4V5H; -.
DR PDBsum; 4V5Y; -.
DR PDBsum; 4V64; -.
DR PDBsum; 4V65; -.
DR PDBsum; 4V66; -.
DR PDBsum; 4V69; -.
DR PDBsum; 4V6C; -.
DR PDBsum; 4V6D; -.
DR PDBsum; 4V6E; -.
DR PDBsum; 4V6K; -.
DR PDBsum; 4V6L; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 4V6N; -.
DR PDBsum; 4V6O; -.
DR PDBsum; 4V6P; -.
DR PDBsum; 4V6Q; -.
DR PDBsum; 4V6R; -.
DR PDBsum; 4V6S; -.
DR PDBsum; 4V6T; -.
DR PDBsum; 4V6V; -.
DR PDBsum; 4V6Y; -.
DR PDBsum; 4V6Z; -.
DR PDBsum; 4V70; -.
DR PDBsum; 4V71; -.
DR PDBsum; 4V72; -.
DR PDBsum; 4V73; -.
DR PDBsum; 4V74; -.
DR PDBsum; 4V75; -.
DR PDBsum; 4V76; -.
DR PDBsum; 4V77; -.
DR PDBsum; 4V78; -.
DR PDBsum; 4V79; -.
DR PDBsum; 4V7A; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7C; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V7I; -.
DR PDBsum; 4V7S; -.
DR PDBsum; 4V7T; -.
DR PDBsum; 4V7U; -.
DR PDBsum; 4V7V; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V9C; -.
DR PDBsum; 4V9D; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 4V9P; -.
DR PDBsum; 4WF1; -.
DR PDBsum; 4WOI; -.
DR PDBsum; 4WWW; -.
DR PDBsum; 4YBB; -.
DR PDBsum; 5ADY; -.
DR PDBsum; 5AFI; -.
DR PDBsum; 5AKA; -.
DR PDBsum; 5GAD; -.
DR PDBsum; 5GAE; -.
DR PDBsum; 5GAF; -.
DR PDBsum; 5GAG; -.
DR PDBsum; 5GAH; -.
DR PDBsum; 5H5U; -.
DR PDBsum; 5IQR; -.
DR PDBsum; 5IT8; -.
DR PDBsum; 5J5B; -.
DR PDBsum; 5J7L; -.
DR PDBsum; 5J88; -.
DR PDBsum; 5J8A; -.
DR PDBsum; 5J91; -.
DR PDBsum; 5JC9; -.
DR PDBsum; 5JTE; -.
DR PDBsum; 5JU8; -.
DR PDBsum; 5KCR; -.
DR PDBsum; 5KCS; -.
DR PDBsum; 5KPS; -.
DR PDBsum; 5KPV; -.
DR PDBsum; 5KPW; -.
DR PDBsum; 5KPX; -.
DR PDBsum; 5L3P; -.
DR PDBsum; 5LZA; -.
DR PDBsum; 5LZB; -.
DR PDBsum; 5LZC; -.
DR PDBsum; 5LZD; -.
DR PDBsum; 5LZE; -.
DR PDBsum; 5LZF; -.
DR PDBsum; 5MDV; -.
DR PDBsum; 5MDW; -.
DR PDBsum; 5MDY; -.
DR PDBsum; 5MDZ; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 5NP6; -.
DR PDBsum; 5NWY; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 5U4I; -.
DR PDBsum; 5U9F; -.
DR PDBsum; 5U9G; -.
DR PDBsum; 5UYK; -.
DR PDBsum; 5UYL; -.
DR PDBsum; 5UYM; -.
DR PDBsum; 5UYN; -.
DR PDBsum; 5UYP; -.
DR PDBsum; 5UYQ; -.
DR PDBsum; 5WDT; -.
DR PDBsum; 5WE4; -.
DR PDBsum; 5WE6; -.
DR PDBsum; 5WFK; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6BY1; -.
DR PDBsum; 6C4H; -.
DR PDBsum; 6ENF; -.
DR PDBsum; 6ENJ; -.
DR PDBsum; 6ENU; -.
DR PDBsum; 6GBZ; -.
DR PDBsum; 6GC0; -.
DR PDBsum; 6GC4; -.
DR PDBsum; 6GC6; -.
DR PDBsum; 6GC8; -.
DR PDBsum; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I0Y; -.
DR PDBsum; 6I7V; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6OFX; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6OGF; -.
DR PDBsum; 6OGG; -.
DR PDBsum; 6OGI; -.
DR PDBsum; 6OM6; -.
DR PDBsum; 6ORE; -.
DR PDBsum; 6ORL; -.
DR PDBsum; 6OST; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 6PC5; -.
DR PDBsum; 6PC6; -.
DR PDBsum; 6PC7; -.
DR PDBsum; 6PC8; -.
DR PDBsum; 6PCH; -.
DR PDBsum; 6PCQ; -.
DR PDBsum; 6PCR; -.
DR PDBsum; 6PCS; -.
DR PDBsum; 6PCT; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6QDW; -.
DR PDBsum; 6QUL; -.
DR PDBsum; 6S0K; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6VU3; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6VYQ; -.
DR PDBsum; 6VYR; -.
DR PDBsum; 6VYS; -.
DR PDBsum; 6VYT; -.
DR PDBsum; 6VYU; -.
DR PDBsum; 6VYW; -.
DR PDBsum; 6VYX; -.
DR PDBsum; 6VYY; -.
DR PDBsum; 6VYZ; -.
DR PDBsum; 6VZ2; -.
DR PDBsum; 6VZ3; -.
DR PDBsum; 6VZ5; -.
DR PDBsum; 6VZ7; -.
DR PDBsum; 6VZJ; -.
DR PDBsum; 6WD0; -.
DR PDBsum; 6WD1; -.
DR PDBsum; 6WD2; -.
DR PDBsum; 6WD3; -.
DR PDBsum; 6WD4; -.
DR PDBsum; 6WD5; -.
DR PDBsum; 6WD6; -.
DR PDBsum; 6WD7; -.
DR PDBsum; 6WD8; -.
DR PDBsum; 6WD9; -.
DR PDBsum; 6WDA; -.
DR PDBsum; 6WDB; -.
DR PDBsum; 6WDC; -.
DR PDBsum; 6WDD; -.
DR PDBsum; 6WDE; -.
DR PDBsum; 6WDF; -.
DR PDBsum; 6WDG; -.
DR PDBsum; 6WDH; -.
DR PDBsum; 6WDI; -.
DR PDBsum; 6WDJ; -.
DR PDBsum; 6WDK; -.
DR PDBsum; 6WDL; -.
DR PDBsum; 6WDM; -.
DR PDBsum; 6WNT; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6WYV; -.
DR PDBsum; 6X6T; -.
DR PDBsum; 6X7F; -.
DR PDBsum; 6X7K; -.
DR PDBsum; 6X9Q; -.
DR PDBsum; 6XDQ; -.
DR PDBsum; 6XDR; -.
DR PDBsum; 6XGF; -.
DR PDBsum; 6XII; -.
DR PDBsum; 6XIJ; -.
DR PDBsum; 6XZ7; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 6Y69; -.
DR PDBsum; 6YS3; -.
DR PDBsum; 6YSR; -.
DR PDBsum; 6YSS; -.
DR PDBsum; 6YST; -.
DR PDBsum; 6YSU; -.
DR PDBsum; 6ZTJ; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 6ZTM; -.
DR PDBsum; 6ZTN; -.
DR PDBsum; 6ZTO; -.
DR PDBsum; 6ZTP; -.
DR PDBsum; 6ZU1; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BL2; -.
DR PDBsum; 7BL3; -.
DR PDBsum; 7BL4; -.
DR PDBsum; 7BL5; -.
DR PDBsum; 7BL6; -.
DR PDBsum; 7BV8; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR PDBsum; 7JSS; -.
DR PDBsum; 7JSW; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7JT1; -.
DR PDBsum; 7JT2; -.
DR PDBsum; 7JT3; -.
DR PDBsum; 7K00; -.
DR PDBsum; 7K50; -.
DR PDBsum; 7K51; -.
DR PDBsum; 7K52; -.
DR PDBsum; 7K53; -.
DR PDBsum; 7K54; -.
DR PDBsum; 7K55; -.
DR PDBsum; 7LV0; -.
DR PDBsum; 7LVK; -.
DR PDBsum; 7N1P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7N2U; -.
DR PDBsum; 7N2V; -.
DR PDBsum; 7N30; -.
DR PDBsum; 7N31; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7NSO; -.
DR PDBsum; 7NSP; -.
DR PDBsum; 7NSQ; -.
DR PDBsum; 7NWT; -.
DR PDBsum; 7NWW; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7OIF; -.
DR PDBsum; 7OIG; -.
DR PDBsum; 7OII; -.
DR PDBsum; 7OIZ; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7OT5; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJS; -.
DR PDBsum; 7PJT; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJW; -.
DR PDBsum; 7PJX; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7PJZ; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7S1G; -.
DR PDBsum; 7S1H; -.
DR PDBsum; 7S1I; -.
DR PDBsum; 7S1J; -.
DR PDBsum; 7S1K; -.
DR PDBsum; 7SS9; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSN; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7SSW; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST6; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P60422; -.
DR SMR; P60422; -.
DR BioGRID; 852132; 4.
DR ComplexPortal; CPX-1944; DnaA-L2 DNA replication initiation inhibitory complex.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35747N; -.
DR IntAct; P60422; 383.
DR STRING; 511145.b3317; -.
DR ChEMBL; CHEMBL2363121; -.
DR iPTMnet; P60422; -.
DR jPOST; P60422; -.
DR PaxDb; P60422; -.
DR PRIDE; P60422; -.
DR EnsemblBacteria; AAC76342; AAC76342; b3317.
DR EnsemblBacteria; BAE77974; BAE77974; BAE77974.
DR GeneID; 60371122; -.
DR GeneID; 67415358; -.
DR GeneID; 947820; -.
DR KEGG; ecj:JW3279; -.
DR KEGG; eco:b3317; -.
DR PATRIC; fig|1411691.4.peg.3414; -.
DR EchoBASE; EB0858; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_6; -.
DR InParanoid; P60422; -.
DR OMA; SCIELRP; -.
DR PhylomeDB; P60422; -.
DR BioCyc; EcoCyc:EG10865-MON; -.
DR BioCyc; MetaCyc:EG10865-MON; -.
DR EvolutionaryTrace; P60422; -.
DR PRO; PR:P60422; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:CAFA.
DR GO; GO:1990082; C:DnaA-L2 complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:CAFA.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..273
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129559"
FT REGION 28..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 230
FT /note="H->Q: Loss of peptidyltransferase activity in
FT reconstituted ribosomes. No change in rRNA binding or
FT assembly into ribosomes."
FT /evidence="ECO:0000269|PubMed:8722025"
FT CONFLICT 232..235
FT /note="HGGG -> GGGH (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7BV8"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6YS3"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6PCQ"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6WNT"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:6PCS"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6PCH"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6XZ7"
SQ SEQUENCE 273 AA; 29860 MW; 1010BDE8D8C68B9B CRC64;
MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT TRHIGGGHKQ
AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE RRYILAPKGL KAGDQIQSGV
DAAIKPGNTL PMRNIPVGST VHNVEMKPGK GGQLARSAGT YVQIVARDGA YVTLRLRSGE
MRKVEADCRA TLGEVGNAEH MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF
GKHPVTPWGV QTKGKKTRSN KRTDKFIVRR RSK
