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1HRD

GLUTAMATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004352molecular_functionglutamate dehydrogenase (NAD+) activity
A0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
A0004354molecular_functionglutamate dehydrogenase (NADP+) activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006537biological_processglutamate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A0019552biological_processL-glutamate catabolic process via 2-hydroxyglutarate
A0055114biological_processobsolete oxidation-reduction process
B0004352molecular_functionglutamate dehydrogenase (NAD+) activity
B0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
B0004354molecular_functionglutamate dehydrogenase (NADP+) activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006537biological_processglutamate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0019552biological_processL-glutamate catabolic process via 2-hydroxyglutarate
B0055114biological_processobsolete oxidation-reduction process
C0004352molecular_functionglutamate dehydrogenase (NAD+) activity
C0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
C0004354molecular_functionglutamate dehydrogenase (NADP+) activity
C0005829cellular_componentcytosol
C0006520biological_processamino acid metabolic process
C0006537biological_processglutamate biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0019552biological_processL-glutamate catabolic process via 2-hydroxyglutarate
C0055114biological_processobsolete oxidation-reduction process
Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpmGGAKgGsdfDP
ChainResidueDetails
ALEU119-PRO132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8263917","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8263917","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 8037659, 8263917
ChainResidueDetails
AASP165
ALYS125

site_idMCSA1
Number of Residues2
DetailsM-CSA 579
ChainResidueDetails
ALYS125electrostatic stabiliser, proton acceptor, proton donor
AASP165proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 579
ChainResidueDetails
BLYS125electrostatic stabiliser, proton acceptor, proton donor
BASP165proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 579
ChainResidueDetails
CLYS125electrostatic stabiliser, proton acceptor, proton donor
CASP165proton acceptor, proton donor

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PDB entries from 2025-12-24

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