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5CTM

Structure of BPu1 beta-lactamase

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue FLC A 301
ChainResidue
AGLN100
AHOH413
AHOH416
AHOH477
AHOH564
ASER101
ATRP136
ASER149
AVAL151
ALYS239
ATHR240
AGLY241
ASER242

site_idAC2
Number of Residues9
Detailsbinding site for residue FLC A 302
ChainResidue
AHIS168
ALYS171
AALA172
AHIS285
AHOH408
AHOH514
AHOH550
AHOH750
AHOH769

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
AARG147
AVAL227
AGLN228
AHOH492
AHOH558
BLYS217
BHOH492

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO A 304
ChainResidue
ALYS217
AHOH476
AHOH498
AHOH501
AHOH510
BARG147
BGLN228
BGLU230

site_idAC5
Number of Residues11
Detailsbinding site for residue FLC B 301
ChainResidue
BGLN100
BSER101
BTRP136
BSER149
BVAL151
BLYS239
BTHR240
BGLY241
BSER242
BHOH419
BHOH459

site_idAC6
Number of Residues5
Detailsbinding site for residue PEG B 302
ChainResidue
BLYS283
BTYR284
BHIS285
BHOH458
BHOH583

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVAnAL
ChainResidueDetails
APRO99-LEU109

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PDB entries from 2024-07-24

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