1NR1
Crystal structure of the R463A mutant of human 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 |
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 | VAL124-PRO137 |
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 | LYS130 | |
| B | LYS130 | |
| C | LYS130 | |
| D | LYS130 | |
| E | LYS130 | |
| F | LYS130 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 78 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00366 |
| Chain | Residue | Details |
| A | GLN88 | |
| A | SER385 | |
| A | LYS391 | |
| A | SER397 | |
| A | ALA463 | |
| B | GLN88 | |
| B | LYS94 | |
| B | LYS118 | |
| B | ASP123 | |
| B | HIS199 | |
| B | HIS213 | |
| A | LYS94 | |
| B | SER217 | |
| B | TYR266 | |
| B | ARG269 | |
| B | SER385 | |
| B | LYS391 | |
| B | SER397 | |
| B | ALA463 | |
| C | GLN88 | |
| C | LYS94 | |
| C | LYS118 | |
| A | LYS118 | |
| C | ASP123 | |
| C | HIS199 | |
| C | HIS213 | |
| C | SER217 | |
| C | TYR266 | |
| C | ARG269 | |
| C | SER385 | |
| C | LYS391 | |
| C | SER397 | |
| C | ALA463 | |
| A | ASP123 | |
| D | GLN88 | |
| D | LYS94 | |
| D | LYS118 | |
| D | ASP123 | |
| D | HIS199 | |
| D | HIS213 | |
| D | SER217 | |
| D | TYR266 | |
| D | ARG269 | |
| D | SER385 | |
| A | HIS199 | |
| D | LYS391 | |
| D | SER397 | |
| D | ALA463 | |
| E | GLN88 | |
| E | LYS94 | |
| E | LYS118 | |
| E | ASP123 | |
| E | HIS199 | |
| E | HIS213 | |
| E | SER217 | |
| A | HIS213 | |
| E | TYR266 | |
| E | ARG269 | |
| E | SER385 | |
| E | LYS391 | |
| E | SER397 | |
| E | ALA463 | |
| F | GLN88 | |
| F | LYS94 | |
| F | LYS118 | |
| F | ASP123 | |
| A | SER217 | |
| F | HIS199 | |
| F | HIS213 | |
| F | SER217 | |
| F | TYR266 | |
| F | ARG269 | |
| F | SER385 | |
| F | LYS391 | |
| F | SER397 | |
| F | ALA463 | |
| A | TYR266 | |
| A | ARG269 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | LYS15 | |
| E | LYS147 | |
| F | LYS15 | |
| F | LYS147 | |
| A | LYS147 | |
| B | LYS15 | |
| B | LYS147 | |
| C | LYS15 | |
| C | LYS147 | |
| D | LYS15 | |
| D | LYS147 | |
| E | LYS15 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | SER26 | |
| E | SER75 | |
| F | SER26 | |
| F | SER75 | |
| A | SER75 | |
| B | SER26 | |
| B | SER75 | |
| C | SER26 | |
| C | SER75 | |
| D | SER26 | |
| D | SER75 | |
| E | SER26 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 54 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P00366 |
| Chain | Residue | Details |
| A | LYS31 | |
| B | LYS31 | |
| B | LYS57 | |
| B | LYS109 | |
| B | LYS310 | |
| B | LYS362 | |
| B | LYS404 | |
| B | LYS450 | |
| B | LYS474 | |
| B | LYS492 | |
| C | LYS31 | |
| A | LYS57 | |
| C | LYS57 | |
| C | LYS109 | |
| C | LYS310 | |
| C | LYS362 | |
| C | LYS404 | |
| C | LYS450 | |
| C | LYS474 | |
| C | LYS492 | |
| D | LYS31 | |
| D | LYS57 | |
| A | LYS109 | |
| D | LYS109 | |
| D | LYS310 | |
| D | LYS362 | |
| D | LYS404 | |
| D | LYS450 | |
| D | LYS474 | |
| D | LYS492 | |
| E | LYS31 | |
| E | LYS57 | |
| E | LYS109 | |
| A | LYS310 | |
| E | LYS310 | |
| E | LYS362 | |
| E | LYS404 | |
| E | LYS450 | |
| E | LYS474 | |
| E | LYS492 | |
| F | LYS31 | |
| F | LYS57 | |
| F | LYS109 | |
| F | LYS310 | |
| A | LYS362 | |
| F | LYS362 | |
| F | LYS404 | |
| F | LYS450 | |
| F | LYS474 | |
| F | LYS492 | |
| A | LYS404 | |
| A | LYS450 | |
| A | LYS474 | |
| A | LYS492 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | TYR82 | |
| B | TYR82 | |
| C | TYR82 | |
| D | TYR82 | |
| E | TYR82 | |
| F | TYR82 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
| Chain | Residue | Details |
| A | LYS94 | |
| B | LYS94 | |
| C | LYS94 | |
| D | LYS94 | |
| E | LYS94 | |
| F | LYS94 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 30 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | LYS118 | |
| B | LYS495 | |
| C | LYS118 | |
| C | LYS134 | |
| C | LYS158 | |
| C | LYS273 | |
| C | LYS495 | |
| D | LYS118 | |
| D | LYS134 | |
| D | LYS158 | |
| D | LYS273 | |
| A | LYS134 | |
| D | LYS495 | |
| E | LYS118 | |
| E | LYS134 | |
| E | LYS158 | |
| E | LYS273 | |
| E | LYS495 | |
| F | LYS118 | |
| F | LYS134 | |
| F | LYS158 | |
| F | LYS273 | |
| A | LYS158 | |
| F | LYS495 | |
| A | LYS273 | |
| A | LYS495 | |
| B | LYS118 | |
| B | LYS134 | |
| B | LYS158 | |
| B | LYS273 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: ADP-ribosylcysteine => ECO:0000269|PubMed:16023112 |
| Chain | Residue | Details |
| A | CYS119 | |
| B | CYS119 | |
| C | CYS119 | |
| D | CYS119 | |
| E | CYS119 | |
| F | CYS119 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 48 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | LYS130 | |
| B | LYS138 | |
| B | LYS293 | |
| B | LYS299 | |
| B | LYS312 | |
| B | LYS337 | |
| B | LYS424 | |
| B | LYS427 | |
| C | LYS130 | |
| C | LYS138 | |
| C | LYS293 | |
| A | LYS138 | |
| C | LYS299 | |
| C | LYS312 | |
| C | LYS337 | |
| C | LYS424 | |
| C | LYS427 | |
| D | LYS130 | |
| D | LYS138 | |
| D | LYS293 | |
| D | LYS299 | |
| D | LYS312 | |
| A | LYS293 | |
| D | LYS337 | |
| D | LYS424 | |
| D | LYS427 | |
| E | LYS130 | |
| E | LYS138 | |
| E | LYS293 | |
| E | LYS299 | |
| E | LYS312 | |
| E | LYS337 | |
| E | LYS424 | |
| A | LYS299 | |
| E | LYS427 | |
| F | LYS130 | |
| F | LYS138 | |
| F | LYS293 | |
| F | LYS299 | |
| F | LYS312 | |
| F | LYS337 | |
| F | LYS424 | |
| F | LYS427 | |
| A | LYS312 | |
| A | LYS337 | |
| A | LYS424 | |
| A | LYS427 | |
| B | LYS130 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER174 | |
| E | SER331 | |
| F | SER174 | |
| F | SER331 | |
| A | SER331 | |
| B | SER174 | |
| B | SER331 | |
| C | SER174 | |
| C | SER331 | |
| D | SER174 | |
| D | SER331 | |
| E | SER174 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00366 |
| Chain | Residue | Details |
| A | LYS333 | |
| E | LYS346 | |
| F | LYS333 | |
| F | LYS346 | |
| A | LYS346 | |
| B | LYS333 | |
| B | LYS346 | |
| C | LYS333 | |
| C | LYS346 | |
| D | LYS333 | |
| D | LYS346 | |
| E | LYS333 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10860 |
| Chain | Residue | Details |
| A | THR357 | |
| B | THR357 | |
| C | THR357 | |
| D | THR357 | |
| E | THR357 | |
| F | THR357 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | TYR459 | |
| B | TYR459 | |
| C | TYR459 | |
| D | TYR459 | |
| E | TYR459 | |
| F | TYR459 |
