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5VPQ

Crystal structure of beta-lactamase from Burkholderia phymatum

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
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 301
ChainResidue
AARG82
AHIS100
AGLU104
AGLY105
AGLU110

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 302
ChainResidue
AHOH448
AHOH544
AGLU195
ALYS198
ALYS198
AHOH424

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 303
ChainResidue
ASER245
ALEU280
AHOH465

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
AGLY229
AASP230
APRO264
AHOH607

site_idAC5
Number of Residues10
Detailsbinding site for residue PO4 A 305
ChainResidue
AVAL90
AVAL91
AALA92
AHIS93
ASER94
ALYS98
AHOH498
AHOH579
AHOH603
BHOH511

site_idAC6
Number of Residues7
Detailsbinding site for residue PO4 B 301
ChainResidue
ALYS260
AHOH456
BASP186
BALA191
BARG194
BHOH407
BHOH458

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO B 302
ChainResidue
BMET73
BASP186
BASP187
BVAL188
BLEU189
BGLY190
BHOH407

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMCSTfKllaVALIL
ChainResidueDetails
APHE54-LEU69

221051

PDB entries from 2024-06-12

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