1NR7
Crystal structure of apo bovine glutamate dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
E | 0006520 | biological_process | amino acid metabolic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
F | 0006520 | biological_process | amino acid metabolic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
G | 0006520 | biological_process | amino acid metabolic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
H | 0006520 | biological_process | amino acid metabolic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
I | 0006520 | biological_process | amino acid metabolic process |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
J | 0006520 | biological_process | amino acid metabolic process |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
K | 0006520 | biological_process | amino acid metabolic process |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
L | 0006520 | biological_process | amino acid metabolic process |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
Functional Information from PROSITE/UniProt
site_id | PS00074 |
Number of Residues | 14 |
Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP |
Chain | Residue | Details |
A | VAL120-PRO133 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 144 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11254391","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12653548","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 108 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 36 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 12 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 48 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 12 |
Details | Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 96 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 24 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 12 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 12 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
A | LYS126 | |
A | ASP168 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
J | LYS126 | |
J | ASP168 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
K | LYS126 | |
K | ASP168 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
L | LYS126 | |
L | ASP168 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
B | LYS126 | |
B | ASP168 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
C | LYS126 | |
C | ASP168 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
D | LYS126 | |
D | ASP168 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
E | LYS126 | |
E | ASP168 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
F | LYS126 | |
F | ASP168 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
G | LYS126 | |
G | ASP168 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
H | LYS126 | |
H | ASP168 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
I | LYS126 | |
I | ASP168 |