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2X87

Crystal Structure of the reconstituted CotA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 601
ChainResidue
AHIS419
ACYS492
AHIS497
AMET502

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 602
ChainResidue
AHIS107
AHIS153
AHIS493
AOH605

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU A 603
ChainResidue
AHIS422
AHIS424
AHIS491
ACU604
AOH605
AHIS155

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CU A 604
ChainResidue
AHIS105
AHIS107
AHIS422
AHIS424
ACU603
AOH605
AHOH2198

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE OH A 605
ChainResidue
AHIS105
AHIS107
AHIS153
AHIS155
AHIS422
AHIS424
AHIS491
AHIS493
ACU602
ACU603
ACU604

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
AASP113
ATYR118
ATYR133
ALYS135
AHOH2575

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
ALYS25
ATYR69
ATHR307
AALA308
ATYR309
AGLU310
AHOH2576

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 703
ChainResidue
AASN74
ALEU76
APRO77
AVAL100
ASER124
ALYS125
AHOH2577

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 704
ChainResidue
AILE12
AGLU188
AGLU244
ATYR250

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 705
ChainResidue
AARG136
AGLU137
AVAL138
APRO247
ALEU343
AHOH2578
AHOH2579

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 706
ChainResidue
AASP268
APRO328
AALA332
AASN333
AHOH2580
AHOH2581

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 707
ChainResidue
ALEU184
ASER186
AGLU348
AHOH2582

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: type 2 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW
ChainResidueDetails
AHIS105
AHIS422

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: type 3 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU
ChainResidueDetails
AHIS107
AHIS153
AHIS155
AHIS424
AHIS491
AHIS493

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU
ChainResidueDetails
AHIS419
ACYS492
AHIS497

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU
ChainResidueDetails
AMET502

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:22481612
ChainResidueDetails
AASP116

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:20200715, ECO:0000305|PubMed:20822511, ECO:0000305|PubMed:22481612
ChainResidueDetails
AGLU498

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PDB entries from 2024-09-11

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