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3OPH

ESBL R164S mutant of SHV-1 beta-lactamase

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 Residues14
DetailsBINDING SITE FOR RESIDUE MA4 A 1
ChainResidue
AGLN32
AHOH416
AHOH425
AHOH486
AHOH487
AHOH572
AGLN39
AARG98
AVAL224
AGLN277
AGLN278
AGLY281
AALA284
AHOH353

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EPE A 293
ChainResidue
AHOH2
ASER70
ATYR105
ASER130
AVAL216
ALYS234
ATHR235
AGLY236
AALA237
AARG244
AHOH515
AHOH619

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MA4 A 294
ChainResidue
ATHR235
AARG244
AILE279

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

226707

PDB entries from 2024-10-30

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