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5EE8

Crystal structure of S02030 boronic acid inhibitor complexed to 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 Residues16
Detailsbinding site for residue ZXM A 301
ChainResidue
AMET69
AGLY236
AALA237
AGLU239
AARG243
AHOH462
AHOH463
AHOH522
ASER70
AASP104
ASER130
AASN132
AGLU166
ATHR167
AASN170
ATHR235

site_idAC2
Number of Residues18
Detailsbinding site for residue MA4 A 302
ChainResidue
AARG93
ALYS94
AILE95
AHIS96
AARG98
AILE221
AVAL224
APRO226
AALA247
AILE261
AILE277
AALA278
AALA282
AGLU286
AMA4303
AHOH422
AHOH423
AHOH440

site_idAC3
Number of Residues11
Detailsbinding site for residue MA4 A 303
ChainResidue
ASER26
AARG98
AASP101
AARG243
AGLN275
AALA278
AGLY279
AALA282
AMA4302
AHOH408
AHOH491

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 2024-07-24

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