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1X8H

The Mono-Zinc Carbapenemase CphA (N220G mutant) Shows a Zn(II)- NH2 ARG Coordination

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACO32
AASP120
AARG121
ACYS221
AHIS263

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 A 2
ChainResidue
AHIS263
AZN401
AHOH403
AHOH404
AHOH410
AASP120
AHIS196
ACYS221
ALYS224

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AARG143
AARG143
ALYS147
ALYS147
AHOH560
AHOH561

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
AARG140
AARG140
AHOH496
AHOH601

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 5
ChainResidue
ALYS97
AARG102
ALYS257
AHOH446
AHOH451
AHOH637

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 6
ChainResidue
AHIS176
AASP177
AGLY178
AASP179
AHOH642

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 7
ChainResidue
ALEU267
AHIS289
AGLY290
AGLU292
AHOH566
AHOH645

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. PdeqVLyGgCILK
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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP120
AASN233

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP120

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PDB entries from 2025-06-11

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