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2JBF

Structure of PBP-A, L158E mutant. Acyl-enzyme complex with penicillin- G.

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 Residues15
DetailsBINDING SITE FOR RESIDUE PNM A 300
ChainResidue
AALA60
ATHR220
AGLY221
AASP222
AHOH2088
AHOH2121
AHOH2157
ASER61
AGLU96
AALA97
ASER122
AASN124
AMET161
ATHR202
ALYS219

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PNM B 300
ChainResidue
BALA60
BSER61
BGLU96
BALA97
BSER122
BASN124
BPRO159
BMET161
BLYS219
BTHR220
BGLY221
BASP222
BHOH2151
BHOH2185
BHOH2202
BHOH2226

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PNM C 300
ChainResidue
CALA60
CSER61
CGLU96
CSER122
CASN124
CMET161
CTHR202
CLYS219
CTHR220
CASP222
CHOH2227
CHOH2260

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PNM D 300
ChainResidue
CGLN26
CARG30
DALA60
DSER61
DGLU96
DALA97
DSER122
DPRO159
DMET161
DLYS219
DTHR220
DGLY221
DASP222

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 2647
ChainResidue
AGLN181
AHOH2129
DASP76
DSER186
DHOH2061

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
ASER61
ALYS64
ASER122
AGLU158

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BSER61
BLYS64
BSER122
BGLU158

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
CSER61
CLYS64
CSER122
CGLU158

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
DSER61
DLYS64
DSER122
DGLU158

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PDB entries from 2024-07-24

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