1EUZ
GLUTAMATE DEHYDROGENASE FROM THERMOCOCCUS PROFUNDUS IN THE UNLIGATED STATE
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 | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) 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 |
| B | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| B | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| B | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) 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 |
| C | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| C | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| C | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| 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 |
| D | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| D | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| D | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006538 | biological_process | L-glutamate catabolic 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 | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| E | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| E | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006538 | biological_process | L-glutamate catabolic 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 | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| F | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| F | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006538 | biological_process | L-glutamate catabolic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 600 |
| Chain | Residue |
| A | SER24 |
| A | GLU25 |
| A | LYS419 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | LYS69 |
| A | GLY70 |
| A | MET90 |
| A | ALA143 |
| A | VAL348 |
| A | SER351 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | THR191 |
| A | ASN222 |
| A | ALA223 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | ARG331 |
| A | HIS388 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 604 |
| Chain | Residue |
| A | ASP413 |
| C | PRO178 |
| C | LEU179 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 605 |
| Chain | Residue |
| A | ASP244 |
| A | SER245 |
| A | LYS264 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 606 |
| Chain | Residue |
| B | PRO178 |
| B | LEU179 |
| B | ARG187 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 607 |
| Chain | Residue |
| B | THR191 |
| B | ASN222 |
| B | ALA223 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 608 |
| Chain | Residue |
| B | ASP244 |
| B | SER245 |
| B | LYS264 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 609 |
| Chain | Residue |
| C | SER245 |
| C | LYS264 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 610 |
| Chain | Residue |
| D | PRO178 |
| D | LEU179 |
| E | ASP413 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 E 611 |
| Chain | Residue |
| E | SER24 |
| E | GLU25 |
| E | LYS419 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 E 612 |
| Chain | Residue |
| E | PRO178 |
| E | LEU179 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 E 613 |
| Chain | Residue |
| E | SER245 |
| E | ARG246 |
| E | GLY247 |
| E | THR280 |
| E | ASN281 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 E 614 |
| Chain | Residue |
| E | ASP244 |
| E | SER245 |
| E | LYS264 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 F 615 |
| Chain | Residue |
| F | PRO178 |
| F | LEU179 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 F 616 |
| Chain | Residue |
| F | ASP244 |
| F | SER245 |
| F | LYS264 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGiivNP |
| Chain | Residue | Details |
| A | LEU99-PRO112 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10011 |
| Chain | Residue | Details |
| A | LYS105 | |
| B | LYS105 | |
| C | LYS105 | |
| D | LYS105 | |
| E | LYS105 | |
| F | LYS105 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY219 | |
| B | GLY219 | |
| C | GLY219 | |
| D | GLY219 | |
| E | GLY219 | |
| F | GLY219 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| A | ASP145 | |
| A | LYS105 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| B | ASP145 | |
| B | LYS105 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| C | ASP145 | |
| C | LYS105 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| D | ASP145 | |
| D | LYS105 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| E | ASP145 | |
| E | LYS105 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| F | ASP145 | |
| F | LYS105 |
