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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
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

221051

PDB entries from 2024-06-12

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