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1L1F

Structure of human glutamate dehydrogenase-apo form

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
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005783cellular_componentendoplasmic reticulum
A0006520biological_processamino acid metabolic process
A0006537biological_processglutamate biosynthetic 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
A0021762biological_processsubstantia nigra development
A0032024biological_processpositive regulation of insulin secretion
A0042803molecular_functionprotein homodimerization activity
A0043531molecular_functionADP binding
A0070403molecular_functionNAD+ binding
A0070728molecular_functionL-leucine 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
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005783cellular_componentendoplasmic reticulum
B0006520biological_processamino acid metabolic process
B0006537biological_processglutamate biosynthetic 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
B0021762biological_processsubstantia nigra development
B0032024biological_processpositive regulation of insulin secretion
B0042803molecular_functionprotein homodimerization activity
B0043531molecular_functionADP binding
B0070403molecular_functionNAD+ binding
B0070728molecular_functionL-leucine 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
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005783cellular_componentendoplasmic reticulum
C0006520biological_processamino acid metabolic process
C0006537biological_processglutamate biosynthetic 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
C0021762biological_processsubstantia nigra development
C0032024biological_processpositive regulation of insulin secretion
C0042803molecular_functionprotein homodimerization activity
C0043531molecular_functionADP binding
C0070403molecular_functionNAD+ binding
C0070728molecular_functionL-leucine 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
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005783cellular_componentendoplasmic reticulum
D0006520biological_processamino acid metabolic process
D0006537biological_processglutamate biosynthetic 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
D0021762biological_processsubstantia nigra development
D0032024biological_processpositive regulation of insulin secretion
D0042803molecular_functionprotein homodimerization activity
D0043531molecular_functionADP binding
D0070403molecular_functionNAD+ binding
D0070728molecular_functionL-leucine 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
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005759cellular_componentmitochondrial matrix
E0005783cellular_componentendoplasmic reticulum
E0006520biological_processamino acid metabolic process
E0006537biological_processglutamate biosynthetic 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
E0021762biological_processsubstantia nigra development
E0032024biological_processpositive regulation of insulin secretion
E0042803molecular_functionprotein homodimerization activity
E0043531molecular_functionADP binding
E0070403molecular_functionNAD+ binding
E0070728molecular_functionL-leucine 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
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005525molecular_functionGTP binding
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005759cellular_componentmitochondrial matrix
F0005783cellular_componentendoplasmic reticulum
F0006520biological_processamino acid metabolic process
F0006537biological_processglutamate biosynthetic 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
F0021762biological_processsubstantia nigra development
F0032024biological_processpositive regulation of insulin secretion
F0042803molecular_functionprotein homodimerization activity
F0043531molecular_functionADP binding
F0070403molecular_functionNAD+ binding
F0070728molecular_functionL-leucine binding
F0072350biological_processtricarboxylic acid metabolic process
Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP
ChainResidueDetails
AVAL124-PRO137

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 Residues84
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00366","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idSWS_FT_FI5
Number of Residues54
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00366","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues30
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsModified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"PubMed","id":"16023112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues48
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00366","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
AASP172
ALYS130

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
BASP172
BLYS130

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
CASP172
CLYS130

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
DASP172
DLYS130

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
EASP172
ELYS130

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
FASP172
FLYS130

242842

PDB entries from 2025-10-08

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