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3F9O

Crystal Structure of the Di-Zinc Carbapenemase CphA from Aeromonas Hydrophila

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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHOH107
AHIS118
AASP120
AHIS196
AHIS263
AZN308
AZN309
AHOH334
AHOH474

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AHIS176
AASP177
AHOH465

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AALA237
AASP238
AVAL239
ALYS240

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
ASER104
ALYS106
AHOH348
AHOH466

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO3 A 5
ChainResidue
ALEU249
ALYS250
ALYS253
ALEU254
AILE256
AHOH365
AHOH421

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO3 A 6
ChainResidue
AARG158
AASP166
AHOH449

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 7
ChainResidue
AHOH19
AASN116
AASN220
ACYS221
AILE222

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 9
ChainResidue
AGLN47
AHOH393

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 10
ChainResidue
ACL11
AZN310

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 11
ChainResidue
ACL10
AHIS289
ALEU293
AZN310

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 12
ChainResidue
AHIS289
AGLY290
AZN310

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 308
ChainResidue
ASO41
AASP120
ACYS221
AHIS263

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 309
ChainResidue
ASO41
AHIS118
AHIS196
AHOH474

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 310
ChainResidue
ACL10
ACL11
ACL12
AHIS289

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

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 2024-07-10

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