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3T9M

Crystal structure of Mutant C221D of 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 Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1
ChainResidue
AALA41
AARG143
ALYS147

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 2
ChainResidue
AASN116
AHIS118
AASP120
AHIS196
AHIS263

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

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
AASP221
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

224931

PDB entries from 2024-09-11

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