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6W34

Crystal Structure of Class A Beta-lactamase from Bacillus cereus

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 Residues9
Detailsbinding site for residue SO4 A 401
ChainResidue
ASER95
ASER153
ALYS257
ASER258
AGLY259
AALA260
AARG266
AHOH564
AHOH641

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 402
ChainResidue
AARG86
AASN88
BLYS164

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 403
ChainResidue
AHIS56
ATYR85
AARG86

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AASP67
ALYS288
AASP289
AGLU290

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
ALYS164
AGLY166
AHOH513

site_idAC6
Number of Residues9
Detailsbinding site for residue SO4 B 401
ChainResidue
BSER95
BSER153
BLYS257
BSER258
BGLY259
BALA260
BARG266
BHOH516
BHOH575

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO B 402
ChainResidue
BARG176
BPRO249
BTHR250

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTyKalaAGVLL
ChainResidueDetails
APHE91-LEU106

221371

PDB entries from 2024-06-19

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