AZUR_PSEAE
ID AZUR_PSEAE Reviewed; 148 AA.
AC P00282;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Azurin;
DE Flags: Precursor;
GN Name=azu; OrderedLocusNames=PA4922;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB
RC 8295 / NRRL B-771;
RX PubMed=2537198; DOI=10.1111/j.1432-1033.1989.tb14540.x;
RA Arvidsson R.H.A., Nordling M., Lundberg L.G.;
RT "The azurin gene from Pseudomonas aeruginosa. Cloning and
RT characterization.";
RL Eur. J. Biochem. 179:195-200(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2116366; DOI=10.1016/0378-1119(90)90434-s;
RA Hoitink C.W.G., Woudt L.P., Turenhout J.C.M., van de Kamp M., Canters G.W.;
RT "Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding
RT gene: comparison with the genes encoding blue copper proteins from
RT Pseudomonas aeruginosa and Alcaligenes faecalis.";
RL Gene 90:15-20(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3100334; DOI=10.1016/0014-5793(87)81579-x;
RA Canters G.W.;
RT "The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a
RT signal peptide. Cloning and sequencing of the azurin gene.";
RL FEBS Lett. 212:168-172(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [5]
RP PROTEIN SEQUENCE OF 21-148.
RC STRAIN=P6009;
RA Ambler R.P.;
RL (In) Preverio A., Pechere J.-F., Coletti-preverio M.-A. (eds.);
RL Developpements recents dans l'etude chimique de la structure des proteines,
RL pp.289-305, INSERM, Paris (1971).
RN [6]
RP PROTEIN SEQUENCE OF 21-41.
RC STRAIN=ATCC 33352 / IATS 05;
RA Charnock C.;
RL Submitted (APR-1996) to UniProtKB.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX PubMed=98639; DOI=10.1016/0022-2836(78)90375-3;
RA Adman E.T., Stenkamp R.E., Sieker L.C., Jensen L.H.;
RT "A crystallographic model for azurin at 3-A resolution.";
RL J. Mol. Biol. 123:35-47(1978).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RA Adman E.T., Jensen L.H.;
RT "Structural features of azurin at 2.7-A resolution.";
RL Isr. J. Chem. 21:8-13(1981).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=1633865; DOI=10.1016/0014-5793(92)80981-l;
RA Nar H., Messerschmidt A., Huber R., van de Kamp M., Canters G.W.;
RT "Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85-A
RT resolution.";
RL FEBS Lett. 306:119-124(1992).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS SER-27 AND SER-130.
RX PubMed=8568881; DOI=10.1006/jmbi.1996.0029;
RA Hammann C., Messerschmidt A., Huber R., Nar H., Gilardi G., Canters G.W.;
RT "X-ray crystal structure of the two site-specific mutants Ile7Ser and
RT Phe110Ser of azurin from Pseudomonas aeruginosa.";
RL J. Mol. Biol. 255:362-366(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT HIS-137.
RX PubMed=9047369; DOI=10.1006/jmbi.1996.0764;
RA Hammann C., van Pouderoyen G., Nar H., Rueth F.-X.G., Messerschmidt A.,
RA Huber R., den Blaauwen T., Canters G.W.;
RT "Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of
RT Pseudomonas aeruginosa azurin.";
RL J. Mol. Biol. 266:357-366(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLU-141.
RX PubMed=9100002; DOI=10.1021/bi962416o;
RA Karlsson B.G., Tsai L.-C., Nar H., Sanders-Loehr J., Bonander N.,
RA Langer V., Sjoelin L.;
RT "X-ray structure determination and characterization of the Pseudomonas
RT aeruginosa azurin mutant Met121Glu.";
RL Biochemistry 36:4089-4095(1997).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=1420141; DOI=10.1021/bi00157a006;
RA van de Kamp M., Canters G.W., Wijmenga S.S., Lommen A., Hilbers C.W.,
RA Nar H., Messerschmidt A., Huber R.;
RT "Complete sequential 1H and 15N nuclear magnetic resonance assignments and
RT solution secondary structure of the blue copper protein azurin from
RT Pseudomonas aeruginosa.";
RL Biochemistry 31:10194-10207(1992).
CC -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC oxidase.
CC -!- INTERACTION:
CC P00282; P00282: azu; NbExp=2; IntAct=EBI-8599567, EBI-8599567;
CC P00282; G3XD89: oprC; NbExp=3; IntAct=EBI-8599567, EBI-26358478;
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR EMBL; X07317; CAA30279.1; -; Genomic_DNA.
DR EMBL; M30389; AAA25730.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08307.1; -; Genomic_DNA.
DR PIR; JQ0644; AZPSCA.
DR RefSeq; NP_253609.1; NC_002516.2.
DR RefSeq; WP_003095591.1; NZ_QZGE01000002.1.
DR PDB; 1AG0; X-ray; 2.40 A; A/B=20-148.
DR PDB; 1AZN; X-ray; 2.60 A; A/B/C/D=21-148.
DR PDB; 1AZR; X-ray; 2.40 A; A/B/C/D=21-148.
DR PDB; 1AZU; X-ray; 2.70 A; A=21-148.
DR PDB; 1BEX; X-ray; 2.30 A; A/B=21-148.
DR PDB; 1CC3; X-ray; 1.65 A; A/B=21-148.
DR PDB; 1E5Y; X-ray; 2.00 A; A/B/C/D=21-148.
DR PDB; 1E5Z; X-ray; 2.00 A; A/B/C/D=21-148.
DR PDB; 1E65; X-ray; 1.85 A; A/B/C/D=21-148.
DR PDB; 1E67; X-ray; 2.14 A; A/B/C/D=21-148.
DR PDB; 1ETJ; X-ray; 2.30 A; A/B/C/D=21-148.
DR PDB; 1EZL; X-ray; 2.00 A; A/B/C/D=21-148.
DR PDB; 1GR7; X-ray; 1.80 A; A/B/C/D=21-148.
DR PDB; 1I53; X-ray; 1.80 A; A/B=21-148.
DR PDB; 1ILS; X-ray; 2.20 A; A/B/C/D=21-148.
DR PDB; 1ILU; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/K/L/M=21-148.
DR PDB; 1JVL; X-ray; 2.00 A; A/B=21-148.
DR PDB; 1JVO; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J/K/L=21-148.
DR PDB; 1JZE; X-ray; 1.60 A; A=21-148.
DR PDB; 1JZF; X-ray; 1.50 A; A=21-148.
DR PDB; 1JZG; X-ray; 1.40 A; A=21-148.
DR PDB; 1JZH; X-ray; 1.70 A; A=21-148.
DR PDB; 1JZI; X-ray; 1.62 A; A/B=21-148.
DR PDB; 1JZJ; X-ray; 1.80 A; A/B=21-148.
DR PDB; 1NZR; X-ray; 2.20 A; A/B/C/D=21-148.
DR PDB; 1R1C; X-ray; 1.90 A; A/B/C/D=21-148.
DR PDB; 1VLX; X-ray; 1.90 A; A/B/C/D=21-148.
DR PDB; 1XB3; X-ray; 1.50 A; A/B=21-148.
DR PDB; 1XB6; X-ray; 1.82 A; A/B=21-148.
DR PDB; 1XB8; X-ray; 2.00 A; A/C=21-148.
DR PDB; 2AZU; X-ray; 1.90 A; A/B/C/D=21-148.
DR PDB; 2FNW; X-ray; 1.40 A; A/B=21-148.
DR PDB; 2FT6; X-ray; 1.25 A; A=21-148.
DR PDB; 2FT7; X-ray; 1.40 A; A=21-148.
DR PDB; 2FT8; X-ray; 1.55 A; A=21-148.
DR PDB; 2FTA; X-ray; 1.61 A; A/B/C/D=21-148.
DR PDB; 2GHZ; X-ray; 1.60 A; A/B=21-148.
DR PDB; 2GI0; X-ray; 1.70 A; A/B=21-148.
DR PDB; 2HX7; X-ray; 1.55 A; A/B=21-148.
DR PDB; 2HX8; X-ray; 1.60 A; A/B=21-148.
DR PDB; 2HX9; X-ray; 1.70 A; A/B=21-148.
DR PDB; 2HXA; X-ray; 2.21 A; A/B=21-148.
DR PDB; 2I7O; X-ray; 1.50 A; A=21-148.
DR PDB; 2I7S; X-ray; 1.35 A; A/B/C/D=21-148.
DR PDB; 2IDF; X-ray; 2.25 A; A/B=21-148.
DR PDB; 2IWE; X-ray; 2.83 A; A/D/G/J=21-148.
DR PDB; 2OJ1; X-ray; 2.30 A; A/B=21-148.
DR PDB; 2TSA; X-ray; 2.20 A; A/B/C/D=21-148.
DR PDB; 2TSB; X-ray; 2.30 A; A/B/C/D=21-148.
DR PDB; 2XV0; X-ray; 1.60 A; A=21-148.
DR PDB; 2XV2; X-ray; 1.60 A; A=21-148.
DR PDB; 2XV3; X-ray; 2.30 A; A/B=21-148.
DR PDB; 3AZU; X-ray; 2.10 A; A/B/C/D=21-148.
DR PDB; 3FPY; X-ray; 2.10 A; A=21-148.
DR PDB; 3FQ1; X-ray; 1.90 A; A=21-148.
DR PDB; 3FQ2; X-ray; 1.91 A; A=21-148.
DR PDB; 3FQY; X-ray; 1.90 A; A=21-148.
DR PDB; 3FS9; X-ray; 1.05 A; A=21-148.
DR PDB; 3FSA; X-ray; 0.98 A; A=21-148.
DR PDB; 3FSV; X-ray; 2.30 A; A=21-148.
DR PDB; 3FSW; X-ray; 2.00 A; A/B/C/D=21-148.
DR PDB; 3FSZ; X-ray; 2.00 A; A/B=21-148.
DR PDB; 3FT0; X-ray; 1.80 A; A/B=21-148.
DR PDB; 3IBO; X-ray; 1.45 A; A/B/C/D=21-148.
DR PDB; 3IN0; X-ray; 2.35 A; A/B/C/D=21-148.
DR PDB; 3IN2; X-ray; 2.60 A; A=21-148.
DR PDB; 3JT2; X-ray; 2.10 A; A/B=21-148.
DR PDB; 3JTB; X-ray; 1.80 A; A/B/C/D=21-148.
DR PDB; 3N2J; X-ray; 1.35 A; A/B/C/D/E/F/G/H/I/J/K/L=21-148.
DR PDB; 3NP3; X-ray; 2.10 A; A=21-148.
DR PDB; 3NP4; X-ray; 2.25 A; A=21-148.
DR PDB; 3OQR; X-ray; 2.40 A; A=21-148.
DR PDB; 3U25; X-ray; 1.18 A; A/B=22-148.
DR PDB; 3UGE; X-ray; 1.70 A; A/B/C/D=21-148.
DR PDB; 4AZU; X-ray; 1.90 A; A/B/C/D=21-148.
DR PDB; 4BWW; X-ray; 1.48 A; A/B/C/D=21-148.
DR PDB; 4HHG; X-ray; 1.60 A; A=21-148.
DR PDB; 4HHW; X-ray; 2.00 A; A/B=21-148.
DR PDB; 4HIP; X-ray; 1.90 A; A/B=21-148.
DR PDB; 4HZ1; X-ray; 2.20 A; A/B/C/D=21-148.
DR PDB; 4JKN; X-ray; 1.54 A; A/B/C/D=21-148.
DR PDB; 4K9J; X-ray; 1.70 A; A=21-148.
DR PDB; 4KO5; X-ray; 1.79 A; A/B=21-148.
DR PDB; 4KO6; X-ray; 1.74 A; A/B/C/D=21-148.
DR PDB; 4KO7; X-ray; 2.07 A; A/B/C/D=21-148.
DR PDB; 4KO9; X-ray; 2.05 A; A/B/C/D=21-148.
DR PDB; 4KOB; X-ray; 1.87 A; A/B/C/D=21-148.
DR PDB; 4KOC; X-ray; 1.46 A; A=21-148.
DR PDB; 4MFH; X-ray; 1.54 A; A/B/C=21-148.
DR PDB; 4QKT; X-ray; 1.64 A; A/B=21-148.
DR PDB; 4QLW; X-ray; 2.00 A; A/B/C/D=21-148.
DR PDB; 4WKX; X-ray; 1.94 A; A/B=21-148.
DR PDB; 5AZU; X-ray; 1.90 A; A/B/C/D=21-148.
DR PDB; 5I26; X-ray; 1.89 A; A/B/C/D=21-148.
DR PDB; 5I28; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=21-148.
DR PDB; 5SYD; X-ray; 2.40 A; A/B=63-148.
DR PDB; 5YT7; X-ray; 1.66 A; A/B/C/D=21-134.
DR PDB; 6GYI; X-ray; 1.60 A; A/B/C/D=21-148.
DR PDB; 6IAV; X-ray; 2.00 A; A/B/C/D=22-148.
DR PDB; 6MJR; X-ray; 2.01 A; A/B/C/D=22-148.
DR PDB; 6MJS; X-ray; 1.85 A; A/B/C/D=22-148.
DR PDB; 6MJT; X-ray; 1.89 A; A/B=22-148.
DR PDBsum; 1AG0; -.
DR PDBsum; 1AZN; -.
DR PDBsum; 1AZR; -.
DR PDBsum; 1AZU; -.
DR PDBsum; 1BEX; -.
DR PDBsum; 1CC3; -.
DR PDBsum; 1E5Y; -.
DR PDBsum; 1E5Z; -.
DR PDBsum; 1E65; -.
DR PDBsum; 1E67; -.
DR PDBsum; 1ETJ; -.
DR PDBsum; 1EZL; -.
DR PDBsum; 1GR7; -.
DR PDBsum; 1I53; -.
DR PDBsum; 1ILS; -.
DR PDBsum; 1ILU; -.
DR PDBsum; 1JVL; -.
DR PDBsum; 1JVO; -.
DR PDBsum; 1JZE; -.
DR PDBsum; 1JZF; -.
DR PDBsum; 1JZG; -.
DR PDBsum; 1JZH; -.
DR PDBsum; 1JZI; -.
DR PDBsum; 1JZJ; -.
DR PDBsum; 1NZR; -.
DR PDBsum; 1R1C; -.
DR PDBsum; 1VLX; -.
DR PDBsum; 1XB3; -.
DR PDBsum; 1XB6; -.
DR PDBsum; 1XB8; -.
DR PDBsum; 2AZU; -.
DR PDBsum; 2FNW; -.
DR PDBsum; 2FT6; -.
DR PDBsum; 2FT7; -.
DR PDBsum; 2FT8; -.
DR PDBsum; 2FTA; -.
DR PDBsum; 2GHZ; -.
DR PDBsum; 2GI0; -.
DR PDBsum; 2HX7; -.
DR PDBsum; 2HX8; -.
DR PDBsum; 2HX9; -.
DR PDBsum; 2HXA; -.
DR PDBsum; 2I7O; -.
DR PDBsum; 2I7S; -.
DR PDBsum; 2IDF; -.
DR PDBsum; 2IWE; -.
DR PDBsum; 2OJ1; -.
DR PDBsum; 2TSA; -.
DR PDBsum; 2TSB; -.
DR PDBsum; 2XV0; -.
DR PDBsum; 2XV2; -.
DR PDBsum; 2XV3; -.
DR PDBsum; 3AZU; -.
DR PDBsum; 3FPY; -.
DR PDBsum; 3FQ1; -.
DR PDBsum; 3FQ2; -.
DR PDBsum; 3FQY; -.
DR PDBsum; 3FS9; -.
DR PDBsum; 3FSA; -.
DR PDBsum; 3FSV; -.
DR PDBsum; 3FSW; -.
DR PDBsum; 3FSZ; -.
DR PDBsum; 3FT0; -.
DR PDBsum; 3IBO; -.
DR PDBsum; 3IN0; -.
DR PDBsum; 3IN2; -.
DR PDBsum; 3JT2; -.
DR PDBsum; 3JTB; -.
DR PDBsum; 3N2J; -.
DR PDBsum; 3NP3; -.
DR PDBsum; 3NP4; -.
DR PDBsum; 3OQR; -.
DR PDBsum; 3U25; -.
DR PDBsum; 3UGE; -.
DR PDBsum; 4AZU; -.
DR PDBsum; 4BWW; -.
DR PDBsum; 4HHG; -.
DR PDBsum; 4HHW; -.
DR PDBsum; 4HIP; -.
DR PDBsum; 4HZ1; -.
DR PDBsum; 4JKN; -.
DR PDBsum; 4K9J; -.
DR PDBsum; 4KO5; -.
DR PDBsum; 4KO6; -.
DR PDBsum; 4KO7; -.
DR PDBsum; 4KO9; -.
DR PDBsum; 4KOB; -.
DR PDBsum; 4KOC; -.
DR PDBsum; 4MFH; -.
DR PDBsum; 4QKT; -.
DR PDBsum; 4QLW; -.
DR PDBsum; 4WKX; -.
DR PDBsum; 5AZU; -.
DR PDBsum; 5I26; -.
DR PDBsum; 5I28; -.
DR PDBsum; 5SYD; -.
DR PDBsum; 5YT7; -.
DR PDBsum; 6GYI; -.
DR PDBsum; 6IAV; -.
DR PDBsum; 6MJR; -.
DR PDBsum; 6MJS; -.
DR PDBsum; 6MJT; -.
DR AlphaFoldDB; P00282; -.
DR BMRB; P00282; -.
DR PCDDB; P00282; -.
DR SMR; P00282; -.
DR DIP; DIP-48787N; -.
DR IntAct; P00282; 6.
DR MINT; P00282; -.
DR STRING; 287.DR97_2273; -.
DR DrugBank; DB06968; 1,1'-HEXANE-1,6-DIYLBIS(1H-IMIDAZOLE).
DR DrugBank; DB02586; 4,7-Dimethyl-[1,10]Phenanthroline.
DR DrugBank; DB04085; Bis(N-maleimidomethyl)ether.
DR DrugBank; DB03492; lambda-bis(2,2'-bipyridine)imidazole osmium (II).
DR DrugBank; DB03871; lambda-bis(2,2'-bipyridine)imidazole ruthenium (II).
DR DrugBank; DB01915; S-Hydroxycysteine.
DR DrugBank; DB04231; Tetra(imidazole)diaquacopper (I).
DR DrugBank; DB03840; Tetra(Imidazole)Diaquacopper (Ii).
DR DrugBank; DB04100; Tricarbonyl(1,10-phenanthroline)rhenium(1+).
DR DrugBank; DB03570; Tris-Hydroxymethyl-Methyl-Ammonium.
DR PaxDb; P00282; -.
DR PRIDE; P00282; -.
DR DNASU; 878046; -.
DR EnsemblBacteria; AAG08307; AAG08307; PA4922.
DR GeneID; 878046; -.
DR KEGG; pae:PA4922; -.
DR PATRIC; fig|208964.12.peg.5155; -.
DR PseudoCAP; PA4922; -.
DR HOGENOM; CLU_112845_1_0_6; -.
DR InParanoid; P00282; -.
DR OMA; MGHNFVL; -.
DR PhylomeDB; P00282; -.
DR BioCyc; PAER208964:G1FZ6-5036-MON; -.
DR SABIO-RK; P00282; -.
DR EvolutionaryTrace; P00282; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IMP:PseudoCAP.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046914; F:transition metal ion binding; IDA:PseudoCAP.
DR GO; GO:0008270; F:zinc ion binding; IMP:PseudoCAP.
DR CDD; cd13922; Azurin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR014068; Azurin.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR008972; Cupredoxin.
DR Pfam; PF00127; Copper-bind; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR02695; azurin; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Electron transport; Metal-binding; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|Ref.5, ECO:0000269|Ref.6"
FT CHAIN 21..148
FT /note="Azurin"
FT /id="PRO_0000002863"
FT DOMAIN 21..148
FT /note="Plastocyanin-like"
FT BINDING 66
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1420141"
FT BINDING 132
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1420141"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1420141"
FT BINDING 141
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT DISULFID 23..46
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3FSA"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4MFH"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1JZJ"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3FSA"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3FSA"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3U25"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3FSA"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3FSA"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3FSA"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:3FSA"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3FSA"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2FT6"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3FSA"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3FSA"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3AZU"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3FSA"
FT TURN 135..140
FT /evidence="ECO:0007829|PDB:3U25"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3FSA"
SQ SEQUENCE 148 AA; 16008 MW; 9C3881D7B6D64B67 CRC64;
MLRKLAAVSL LSLLSAPLLA AECSVDIQGN DQMQFNTNAI TVDKSCKQFT VNLSHPGNLP
KNVMGHNWVL STAADMQGVV TDGMASGLDK DYLKPDDSRV IAHTKLIGSG EKDSVTFDVS
KLKEGEQYMF FCTFPGHSAL MKGTLTLK
