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3VFH

BlaC E166A CDC-1 Acyl-Intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
C0005576cellular_componentextracellular region
C0005886cellular_componentplasma membrane
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0030655biological_processbeta-lactam antibiotic catabolic process
C0042597cellular_componentperiplasmic space
C0046677biological_processresponse to antibiotic
D0005576cellular_componentextracellular region
D0005886cellular_componentplasma membrane
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0030655biological_processbeta-lactam antibiotic catabolic process
D0042597cellular_componentperiplasmic space
D0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 301
ChainResidue
ASER70
ASER130
ATHR216
ATHR235
ATHR237
BGLN110
BGLN111

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 302
ChainResidue
AARG213
AHOH431
AASP124
AARG128

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 303
ChainResidue
AARG171
AASP240
AHOH416
BSER99
BGLN114

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CD6 B 301
ChainResidue
AGLN111
BCYS69
BSER70
BSER130
BASN170
BARG220
BTHR235
BGLY236
BTHR237

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 302
ChainResidue
BASP124
BARG128
BARG213

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CD6 C 301
ChainResidue
CSER70
CILE105
CSER130
CASN170
CTHR235
CGLY236
CTHR237
CGLY238
CHOH403

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 C 302
ChainResidue
CASP124
CARG128
CARG213

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 D 301
ChainResidue
CGLN111
DSER70
DSER130
DTHR216
DTHR235
DTHR237

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 D 302
ChainResidue
DASP124
DARG128
DARG213

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Increases nucleophilicity of active site Ser","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site","evidences":[{"source":"PubMed","id":"24023821","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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