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2A3U

Crystal structure of sulbactam bound to E166A variant of SHV-1 beta-lactamase

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 Residues9
DetailsBINDING SITE FOR RESIDUE TSL A 501
ChainResidue
AMET69
ASER70
AASP104
AASN132
ATHR167
AASN170
AGLY236
AALA237
AEPE600

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MA4 A 400
ChainResidue
AARG93
AHIS96
AARG98
AVAL224
APRO226
AALA248
AVAL261
AILE263
AALA280
AALA284
AGLU288
AHOH634
AHOH730
AHOH739
AHOH804
AHOH838
AHOH857

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MA4 A 401
ChainResidue
AARG244
AILE279
AALA280

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE A 600
ChainResidue
ASER70
ASER130
AVAL216
ALYS234
ATHR235
AGLY236
AARG244
ATSL501

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
AALA166

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AALA166
ALYS73
ASER130
ASER70

226707

PDB entries from 2024-10-30

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