Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1NR7

Crystal structure of apo bovine glutamate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0006520biological_processamino acid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0006520biological_processamino acid metabolic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0006520biological_processamino acid metabolic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D0006520biological_processamino acid metabolic process
D0016491molecular_functionoxidoreductase activity
D0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E0006520biological_processamino acid metabolic process
E0016491molecular_functionoxidoreductase activity
E0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F0006520biological_processamino acid metabolic process
F0016491molecular_functionoxidoreductase activity
F0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
G0006520biological_processamino acid metabolic process
G0016491molecular_functionoxidoreductase activity
G0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
H0006520biological_processamino acid metabolic process
H0016491molecular_functionoxidoreductase activity
H0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
I0006520biological_processamino acid metabolic process
I0016491molecular_functionoxidoreductase activity
I0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
J0006520biological_processamino acid metabolic process
J0016491molecular_functionoxidoreductase activity
J0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
K0006520biological_processamino acid metabolic process
K0016491molecular_functionoxidoreductase activity
K0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
L0006520biological_processamino acid metabolic process
L0016491molecular_functionoxidoreductase activity
L0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
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 Residues12
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues144
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11254391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12653548","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues24
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues24
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues108
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues36
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues12
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues48
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues12
DetailsModified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues96
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues24
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues12
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues12
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
ALYS126
AASP168
site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
JLYS126
JASP168
site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
KLYS126
KASP168
site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
LLYS126
LASP168
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
BLYS126
BASP168
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
CLYS126
CASP168
site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
DLYS126
DASP168
site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
ELYS126
EASP168
site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
FLYS126
FASP168
site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
GLYS126
GASP168
site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
HLYS126
HASP168
site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
ILYS126
IASP168

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon