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4WZ4

Crystal structure of P. aeruginosa AmpC

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 Residues10
Detailsbinding site for residue GOL A 401
ChainResidue
AGLU269
AHOH888
AARG273
AALA276
AGLN277
AASP280
AGLN321
APRO322
AHOH516
AHOH553

site_idAC2
Number of Residues13
Detailsbinding site for residue 3VU A 402
ChainResidue
ASER90
AGLN146
ATYR177
AASN179
ATYR249
ATHR343
AGLY344
ASER345
AASN373
AARG376
AHOH712
AHOH751
AHOH859

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
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10102","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00811","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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