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6UR3

Serendipitous Discovery of Aryl Boronic Acids as beta-Lactamase Inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue QFP A 401
ChainResidue
ASER90
ATYR177
ATYR249
ALYS342
ATHR343
AGLY344
ASER345
AEDO402
AHOH597

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 402
ChainResidue
AARG175
ATYR177
AGLU299
AMET318
ALYS342
AQFP401
AHOH503
AHOH644

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 403
ChainResidue
AGLU269
AALA276
AASP280
APRO322

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 404
ChainResidue
AGLN146
APHE147
AASN179

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK
ChainResidueDetails
APHE86-LYS93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102
ChainResidueDetails
ASER90

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR177

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS342

218853

PDB entries from 2024-04-24

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