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1W7F

Crystal structure of the class A beta-lactamase BS3 inhibited with isocitrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ICT A1291
ChainResidue
AALA69
AARG244
AHOH2035
AHOH2107
AHOH2119
ASER70
ALYS73
ATYR105
ASER130
ATHR216
ATHR235
AGLY236
AALA237

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNRTVT
ChainResidueDetails
APHE47-THR59

site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Acyl-ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AGLU166
ALYS73
ASER130
ASER70

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BGLU166
BLYS73
BSER130
BSER70

246704

PDB entries from 2025-12-24

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