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3OPP

ESBL R164S mutant of SHV-1 beta-lactamase complexed with SA2-13

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase 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 SA2 A 1
ChainResidue
AMET69
AALA237
AARG244
AHOH401
AHOH404
AHOH409
AHOH430
ASER70
AGLN100
ATYR105
ASER130
AASN132
ALYS234
ATHR235
AGLY236

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MA4 A 293
ChainResidue
AHOH2
AARG93
ALYS94
AILE95
AHIS96
AARG98
AILE221
AVAL224
APRO226
AALA248
AILE263
AALA280
AALA284
AGLU288
AHOH378
AHOH434
AHOH513
AHOH517

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MA4 A 294
ChainResidue
AALA217
AARG244

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; acyl-ester intermediate => ECO:0000250|UniProtKB:A0A5R8T042, ECO:0000255|PROSITE-ProRule:PRU10101
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU168

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A5R8T042
ChainResidueDetails
ALYS73
ASER130
AGLU166

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PDB entries from 2024-07-17

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