2YFQ
Crystal structure of Glutamate dehydrogenase from Peptoniphilus asaccharolyticus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| A | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| 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 |
| A | 0019552 | biological_process | L-glutamate catabolic process via 2-hydroxyglutarate |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| B | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| 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 |
| B | 0019552 | biological_process | L-glutamate catabolic process via 2-hydroxyglutarate |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1422 |
| Chain | Residue |
| A | LYS70 |
| A | GLY71 |
| A | MET91 |
| A | ALA144 |
| A | VAL352 |
| A | SER355 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1423 |
| Chain | Residue |
| A | PRO178 |
| A | VAL179 |
| A | ARG187 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1422 |
| Chain | Residue |
| B | VAL179 |
| B | ARG187 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1423 |
| Chain | Residue |
| B | LYS70 |
| B | GLY71 |
| B | MET91 |
| B | ALA144 |
| B | VAL352 |
| B | SER355 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGicvDP |
| Chain | Residue | Details |
| A | LEU100-PRO113 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10011 |
| Chain | Residue | Details |
| A | LYS106 | |
| B | LYS106 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS70 | |
| B | SER355 | |
| A | LYS94 | |
| A | THR191 | |
| A | ASN222 | |
| A | SER355 | |
| B | LYS70 | |
| B | LYS94 | |
| B | THR191 | |
| B | ASN222 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for catalysis => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP146 | |
| B | ASP146 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for nucleotide recognition => ECO:0000269|PubMed:17850332 |
| Chain | Residue | Details |
| A | GLU243 | |
| B | GLU243 |
