1GTM
STRUCTURE OF GLUTAMATE DEHYDROGENASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004352 | molecular_function | L-glutamate dehydrogenase (NAD+) activity |
| A | 0004353 | molecular_function | L-glutamate dehydrogenase [NAD(P)+] activity |
| A | 0004354 | molecular_function | L-glutamate dehydrogenase (NADP+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006538 | biological_process | L-glutamate catabolic 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 | 0004352 | molecular_function | L-glutamate dehydrogenase (NAD+) activity |
| B | 0004353 | molecular_function | L-glutamate dehydrogenase [NAD(P)+] activity |
| B | 0004354 | molecular_function | L-glutamate dehydrogenase (NADP+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006538 | biological_process | L-glutamate catabolic 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 | 0004352 | molecular_function | L-glutamate dehydrogenase (NAD+) activity |
| C | 0004353 | molecular_function | L-glutamate dehydrogenase [NAD(P)+] activity |
| C | 0004354 | molecular_function | L-glutamate dehydrogenase (NADP+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006538 | biological_process | L-glutamate catabolic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 420 |
| Chain | Residue |
| A | ASP244 |
| A | SER245 |
| A | LYS264 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 420 |
| Chain | Residue |
| B | GLY221 |
| B | ASN222 |
| B | ALA223 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 420 |
| Chain | Residue |
| C | GLY221 |
| C | ASN222 |
| C | ALA223 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 421 |
| Chain | Residue |
| B | ASP244 |
| B | SER245 |
| B | LYS246 |
| B | LYS264 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 421 |
| Chain | Residue |
| A | GLY221 |
| A | ASN222 |
| A | ALA223 |
| A | HOH482 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 421 |
| Chain | Residue |
| C | ASP244 |
| C | SER245 |
| C | LYS246 |
| C | LYS264 |
| C | HOH437 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGiivDP |
| Chain | Residue | Details |
| A | LEU98-PRO111 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| 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 | LYS104 | |
| A | ASP144 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| B | LYS104 | |
| B | ASP144 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| C | LYS104 | |
| C | ASP144 |
