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3JD0

Glutamate dehydrogenase in complex with GTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004352molecular_functionglutamate dehydrogenase (NAD+) activity
A0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
A0004354molecular_functionglutamate dehydrogenase (NADP+) activity
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005783cellular_componentendoplasmic reticulum
A0006520biological_processamino acid metabolic process
A0006538biological_processL-glutamate catabolic process
A0006541biological_processglutamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0072350biological_processtricarboxylic acid metabolic process
B0000166molecular_functionnucleotide binding
B0004352molecular_functionglutamate dehydrogenase (NAD+) activity
B0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
B0004354molecular_functionglutamate dehydrogenase (NADP+) activity
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005783cellular_componentendoplasmic reticulum
B0006520biological_processamino acid metabolic process
B0006538biological_processL-glutamate catabolic process
B0006541biological_processglutamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
B0072350biological_processtricarboxylic acid metabolic process
C0000166molecular_functionnucleotide binding
C0004352molecular_functionglutamate dehydrogenase (NAD+) activity
C0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
C0004354molecular_functionglutamate dehydrogenase (NADP+) activity
C0005524molecular_functionATP binding
C0005525molecular_functionGTP binding
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0005783cellular_componentendoplasmic reticulum
C0006520biological_processamino acid metabolic process
C0006538biological_processL-glutamate catabolic process
C0006541biological_processglutamine metabolic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0042802molecular_functionidentical protein binding
C0072350biological_processtricarboxylic acid metabolic process
D0000166molecular_functionnucleotide binding
D0004352molecular_functionglutamate dehydrogenase (NAD+) activity
D0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
D0004354molecular_functionglutamate dehydrogenase (NADP+) activity
D0005524molecular_functionATP binding
D0005525molecular_functionGTP binding
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0005783cellular_componentendoplasmic reticulum
D0006520biological_processamino acid metabolic process
D0006538biological_processL-glutamate catabolic process
D0006541biological_processglutamine metabolic process
D0016491molecular_functionoxidoreductase activity
D0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D0042802molecular_functionidentical protein binding
D0072350biological_processtricarboxylic acid metabolic process
E0000166molecular_functionnucleotide binding
E0004352molecular_functionglutamate dehydrogenase (NAD+) activity
E0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
E0004354molecular_functionglutamate dehydrogenase (NADP+) activity
E0005524molecular_functionATP binding
E0005525molecular_functionGTP binding
E0005739cellular_componentmitochondrion
E0005743cellular_componentmitochondrial inner membrane
E0005783cellular_componentendoplasmic reticulum
E0006520biological_processamino acid metabolic process
E0006538biological_processL-glutamate catabolic process
E0006541biological_processglutamine metabolic process
E0016491molecular_functionoxidoreductase activity
E0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E0042802molecular_functionidentical protein binding
E0072350biological_processtricarboxylic acid metabolic process
F0000166molecular_functionnucleotide binding
F0004352molecular_functionglutamate dehydrogenase (NAD+) activity
F0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
F0004354molecular_functionglutamate dehydrogenase (NADP+) activity
F0005524molecular_functionATP binding
F0005525molecular_functionGTP binding
F0005739cellular_componentmitochondrion
F0005743cellular_componentmitochondrial inner membrane
F0005783cellular_componentendoplasmic reticulum
F0006520biological_processamino acid metabolic process
F0006538biological_processL-glutamate catabolic process
F0006541biological_processglutamine metabolic process
F0016491molecular_functionoxidoreductase activity
F0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F0042802molecular_functionidentical protein binding
F0072350biological_processtricarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTP A 601
ChainResidue
AILE212
AARG261
ATYR262
AARG265
AGLU292
ALYS446

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTP B 601
ChainResidue
BARG265
BGLU292
BLYS446
BILE212
BARG261
BTYR262

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTP C 601
ChainResidue
CILE212
CARG261
CTYR262
CARG265
CGLU292
CLYS446

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTP D 601
ChainResidue
DILE212
DARG261
DTYR262
DARG265
DGLU292
DLYS446

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTP E 601
ChainResidue
EILE212
EARG261
ETYR262
EARG265
EGLU292
ELYS446

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTP F 601
ChainResidue
FILE212
FARG261
FTYR262
FARG265
FGLU292
FLYS446

Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP
ChainResidueDetails
AVAL120-PRO133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues72
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11254391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12653548","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues54
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues18
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues24
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsModified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues48
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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