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5CTN

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 Residues11
Detailsbinding site for residue 5R7 A 301
ChainResidue
AGLN100
AHOH469
AHOH485
ASER101
ATRP136
ASER149
AVAL151
AGLY241
ASER242
ATHR269
AHOH439

site_idAC2
Number of Residues8
Detailsbinding site for residue FLC A 302
ChainResidue
AHIS168
AALA172
AHIS285
AHOH414
AHOH441
AHOH495
AHOH520
AHOH539

site_idAC3
Number of Residues15
Detailsbinding site for Di-peptide 5R7 B 300 and SER B 101
ChainResidue
BPRO99
BGLN100
BTHR102
BPHE103
BLYS104
BGLU132
BTRP136
BSER149
BVAL151
BLEU189
BLYS239
BTHR240
BGLY241
BSER242
BHOH404

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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