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2QDS

Crystal Structure of the Zinc Carbapenemase CPHA in Complex with the Inhibitor D-Captopril

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AASP120
ACYS221
AHIS263
AMCO501

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AHOH779
ASER104
AARG105
ALYS106
AHOH622
AHOH768

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
ALYS129
AARG140
AASN173
ALYS302
AHOH712
AHOH774

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
ALYS147
ALYS147
ALEU171
AHOH754

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ALYS97
ALEU98
AARG102
ALYS257
AHOH647
AHOH652
AHOH780

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MCO A 501
ChainResidue
AHIS118
ATHR119
AASP120
ALEU161
AHIS196
ACYS221
AASN233
AHIS263
AZN401
AHOH608
AHOH609

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 605
ChainResidue
AHIS176
AASP177
AGLY178
AASP179

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 606
ChainResidue
AASP179
AARG188
APHE190
ATYR204
AHOH686

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. InTNyHTDraGGnaywksi.G
ChainResidueDetails
AILE113-GLY133

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PdeqVLyGnCILK
ChainResidueDetails
APRO209-LYS224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:18563261, ECO:0000269|PubMed:19651913, ECO:0000269|PubMed:20527888
ChainResidueDetails
AASP120
ACYS221
AHIS263

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15588826
ChainResidueDetails
ATHR157

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:18563261, ECO:0000269|PubMed:20527888
ChainResidueDetails
AHIS196

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:20527888
ChainResidueDetails
ALYS224

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:18563261
ChainResidueDetails
AASN233

221051

PDB entries from 2024-06-12

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