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5E2G

Crystal Structure of D-alanine Carboxypeptidase AmpC from Burkholderia cenocepacia

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SCN A 401
ChainResidue
ATHR261
AGLN268
APRO270

site_idAC2
Number of Residues1
Detailsbinding site for residue SCN A 402
ChainResidue
AHOH694

site_idAC3
Number of Residues6
Detailsbinding site for residue ACY A 404
ChainResidue
BHOH504
APRO276
AHOH504
BLEU279
BGLU342
BLYS346

site_idAC4
Number of Residues3
Detailsbinding site for residue SCN B 401
ChainResidue
BARG256
BTHR261
BHOH659

site_idAC5
Number of Residues1
Detailsbinding site for residue SCN B 403
ChainResidue
BARG172

site_idAC6
Number of Residues5
Detailsbinding site for residue ACY B 404
ChainResidue
ALEU279
AGLU342
ALYS346
BPRO276
BHOH555

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK
ChainResidueDetails
APHE55-LYS62

238268

PDB entries from 2025-07-02

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