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1KDS

X-ray crystal structure of AmpC beta-lactamase from E. coli in complex with the inhibitor 3-nitrophenylboronic acid

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 Residues7
DetailsBINDING SITE FOR RESIDUE NPB A 364
ChainResidue
ASER64
ATYR150
AASN152
ATYR221
AGLY317
AALA318
AHOH400

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NPB B 364
ChainResidue
BASN152
BTYR221
BALA318
BHOH402
BHOH505
BSER64
BTYR150

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:6795623
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS315
BLYS315

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PDB entries from 2024-05-01

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