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2J9O

Structure of PBP-A, L158E mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
C0008800molecular_functionbeta-lactamase activity
C0017001biological_processantibiotic catabolic process
C0030655biological_processbeta-lactam antibiotic catabolic process
C0046677biological_processresponse to antibiotic
D0008800molecular_functionbeta-lactamase activity
D0017001biological_processantibiotic catabolic process
D0030655biological_processbeta-lactam antibiotic catabolic process
D0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1276
ChainResidue
BSER61
BALA97
BSER122
BTHR220
BGLY221
BASP222
BHOH2381
BHOH2382

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 1277
ChainResidue
DSER122
DTHR220
DGLY221
DASP222
DHOH2370
DHOH2371
DSER61

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL C 1275
ChainResidue
CSER61
CSER122
CTHR202
CLYS219
CTHR220
CGLY221
CASP222
CHOH2375
CHOH2444
CHOH2445
CHOH2446

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FNLDSGASLNVG
ChainResidueDetails
APHE41-GLY52

221051

PDB entries from 2024-06-12

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