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4WYY

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
AARG175
AHOH708
ATYR177
AGLU299
AMET318
ALYS342
ATHR343
A3VT406
AHOH678
AHOH704

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
ATHR316
AALA319
AASN373
A3VT406
AHOH732
AHOH744
AHOH762
AHOH846

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 403
ChainResidue
AASP160
ATRP275
AHOH502
AHOH532
AHOH544

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL A 404
ChainResidue
AGLU269
AARG273
AALA276
AGLN277
AASP280
AGLN321
APRO322
AHOH514
AHOH518

site_idAC5
Number of Residues3
Detailsbinding site for residue DMS A 405
ChainResidue
AASN347
AASN370
A3VT406

site_idAC6
Number of Residues14
Detailsbinding site for residue 3VT A 406
ChainResidue
ASER90
ATYR177
AASN179
ATYR249
ATHR343
AGLY344
ASER345
ATHR346
AASN373
AARG376
AGOL401
AGOL402
ADMS405
AHOH856

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

220113

PDB entries from 2024-05-22

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