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3K92

Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG

Functional Information from GO Data
ChainGOidnamespacecontents
A0004352molecular_functionglutamate dehydrogenase (NAD+) activity
A0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
A0005515molecular_functionprotein binding
A0006520biological_processamino acid metabolic process
A0006538biological_processglutamate catabolic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A0055114biological_processobsolete oxidation-reduction process
B0004352molecular_functionglutamate dehydrogenase (NAD+) activity
B0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
B0005515molecular_functionprotein binding
B0006520biological_processamino acid metabolic process
B0006538biological_processglutamate catabolic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0055114biological_processobsolete oxidation-reduction process
C0004352molecular_functionglutamate dehydrogenase (NAD+) activity
C0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
C0005515molecular_functionprotein binding
C0006520biological_processamino acid metabolic process
C0006538biological_processglutamate catabolic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0055114biological_processobsolete oxidation-reduction process
D0004352molecular_functionglutamate dehydrogenase (NAD+) activity
D0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
D0005515molecular_functionprotein binding
D0006520biological_processamino acid metabolic process
D0006538biological_processglutamate catabolic process
D0016491molecular_functionoxidoreductase activity
D0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D0055114biological_processobsolete oxidation-reduction process
E0004352molecular_functionglutamate dehydrogenase (NAD+) activity
E0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
E0005515molecular_functionprotein binding
E0006520biological_processamino acid metabolic process
E0006538biological_processglutamate catabolic process
E0016491molecular_functionoxidoreductase activity
E0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E0055114biological_processobsolete oxidation-reduction process
F0004352molecular_functionglutamate dehydrogenase (NAD+) activity
F0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
F0005515molecular_functionprotein binding
F0006520biological_processamino acid metabolic process
F0006538biological_processglutamate catabolic process
F0016491molecular_functionoxidoreductase activity
F0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 425
ChainResidue
ALEU131
AASN160
AGLN162

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG C 425
ChainResidue
CLEU131
CASN160

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG D 425
ChainResidue
DASN160

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG E 425
ChainResidue
ELEU131
EASN160

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG F 425
ChainResidue
FGLN162
FILE163
FASN160

Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGiicDP
ChainResidueDetails
ALEU110-PRO123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10011
ChainResidueDetails
ALYS116
BLYS116
CLYS116
DLYS116
ELYS116
FLYS116

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS80
BSER358
CLYS80
CLYS104
CTHR200
CASN231
CSER358
DLYS80
DLYS104
DTHR200
DASN231
ALYS104
DSER358
ELYS80
ELYS104
ETHR200
EASN231
ESER358
FLYS80
FLYS104
FTHR200
FASN231
ATHR200
FSER358
AASN231
ASER358
BLYS80
BLYS104
BTHR200
BASN231

site_idSWS_FT_FI3
Number of Residues6
DetailsSITE: Important for catalysis => ECO:0000250
ChainResidueDetails
AASP156
BASP156
CASP156
DASP156
EASP156
FASP156

223166

PDB entries from 2024-07-31

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