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5TFQ

Crystal structure of a representative of class A beta-lactamase from Bacteroides cellulosilyticus DSM 14838

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue PO4 A 301
ChainResidue
AARG3
AHOH474
AHOH561
ASER48
ASER112
ALYS215
ATHR216
AGLY217
ASER218
APO4302
AHOH413

site_idAC2
Number of Residues9
Detailsbinding site for residue PO4 A 302
ChainResidue
AGLN7
AGLY198
ALYS201
ATHR216
APO4301
AHOH431
AHOH440
AHOH644
AHOH645

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
ALYS106
AALA190
AGLU194
AHOH465
AHOH672

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 304
ChainResidue
AASP32
AGLU33
ATHR34
AARG169
AHOH489
AHOH553
AHOH691

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpLLSVfKfhvGLAVL
ChainResidueDetails
APHE44-LEU59

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PDB entries from 2024-10-09

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