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4FH2

Structure of s70c beta-lactamase bound to sulbactam

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MA4 A 301
ChainResidue
AARG93
AILE263
AALA280
AALA284
AHOH415
AHOH475
AHOH585
ALYS94
AILE95
AHIS96
AARG98
AVAL224
APRO226
AILE231
AVAL261

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MA4 A 302
ChainResidue
AARG244
AILE279

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 0RN A 303
ChainResidue
ACYS70
ASER130
AVAL216
ATHR235
AGLY236
AALA237
AARG244
AHOH535
AHOH600

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"UniProtKB","id":"A0A5R8T042","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10101","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A5R8T042","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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