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4OLG

Crystal structure of AmpC beta-lactamase in complex with covalently bound N-formyl 7-aminocephalosporanic 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 Residues14
DetailsBINDING SITE FOR RESIDUE 2TV A 401
ChainResidue
ASER64
AHOH675
AHOH677
AHOH679
AHOH698
AHOH704
ALEU119
ATYR150
AILE291
ATHR316
AGLY317
AALA318
AASN346
AHOH563

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AHIS186
AHOH647
AHOH689
AHOH711
BLYS290

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2TV B 401
ChainResidue
BSER64
BLEU119
BTYR150
BASN289
BLEU293
BGLY317
BALA318
BASN346
BHOH649
BHOH655
BHOH680
BHOH681
BHOH682

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

218853

PDB entries from 2024-04-24

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