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1KGG

STRUCTURE OF BETA-LACTAMASE GLU166GLN:ASN170ASP MUTANT

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 292
ChainResidue
ASER70
ASER130
ALYS234
ASER235
AGLY236
AGLN237

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS234

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AGLN166
ALYS73
ASER130
ASER70

223166

PDB entries from 2024-07-31

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