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2P9V

Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor

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
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 1
ChainResidue
AHIS186
AHOH676
AHOH702
AHOH707
AHOH782
BLYS290

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
BPHE60-LYS67
APHE60-LYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:6795623
ChainResidueDetails
BSER64

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BTYR150

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BLYS315

220113

PDB entries from 2024-05-22

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