3AOG
Crystal structure of glutamate dehydrogenase (GdhB) from Thermus thermophilus (Glu bound form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| C | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] 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 | 0000166 | molecular_function | nucleotide binding |
| D | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| D | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] 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 | 0000166 | molecular_function | nucleotide binding |
| E | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| E | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] 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 | 0000166 | molecular_function | nucleotide binding |
| F | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| F | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] 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 |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| G | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0006538 | biological_process | L-glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
| H | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| H | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0006538 | biological_process | L-glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
| I | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| I | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| I | 0006520 | biological_process | amino acid metabolic process |
| I | 0006538 | biological_process | L-glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
| J | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| J | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| J | 0006520 | biological_process | amino acid metabolic process |
| J | 0006538 | biological_process | L-glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
| K | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| K | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| K | 0006520 | biological_process | amino acid metabolic process |
| K | 0006538 | biological_process | L-glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
| L | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| L | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| L | 0006520 | biological_process | amino acid metabolic process |
| L | 0006538 | biological_process | L-glutamate catabolic 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 PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GLU A 500 |
| Chain | Residue |
| A | GLY80 |
| A | HOH671 |
| A | HOH1052 |
| A | MET99 |
| A | LYS114 |
| A | ALA152 |
| A | PRO153 |
| A | ASP154 |
| A | ARG194 |
| A | VAL354 |
| A | SER357 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU A 425 |
| Chain | Residue |
| A | ALA73 |
| A | ARG417 |
| A | ARG420 |
| A | GLY421 |
| A | LEU422 |
| A | TYR423 |
| A | HOH469 |
| B | ARG135 |
| E | ASP167 |
| E | MET171 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLU B 500 |
| Chain | Residue |
| B | GLY80 |
| B | MET99 |
| B | LYS114 |
| B | ALA152 |
| B | PRO153 |
| B | ASP154 |
| B | ARG194 |
| B | VAL354 |
| B | SER357 |
| B | HOH835 |
| B | HOH1737 |
| B | HOH1812 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU B 425 |
| Chain | Residue |
| A | ARG135 |
| B | THR72 |
| B | ALA73 |
| B | ARG420 |
| B | GLY421 |
| B | LEU422 |
| B | TYR423 |
| B | HOH440 |
| B | HOH1358 |
| D | ASP167 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU C 500 |
| Chain | Residue |
| C | GLY80 |
| C | MET99 |
| C | LYS114 |
| C | ALA152 |
| C | PRO153 |
| C | ASP154 |
| C | SER357 |
| C | HOH453 |
| C | HOH746 |
| C | HOH1253 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GLU C 425 |
| Chain | Residue |
| A | ASP167 |
| A | MET171 |
| C | ALA73 |
| C | ARG417 |
| C | ARG420 |
| C | GLY421 |
| C | LEU422 |
| C | TYR423 |
| C | HOH435 |
| C | HOH1188 |
| D | ARG135 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU D 500 |
| Chain | Residue |
| D | GLY80 |
| D | MET99 |
| D | LYS114 |
| D | PRO153 |
| D | ASP154 |
| D | ARG194 |
| D | SER357 |
| D | HOH431 |
| D | HOH1801 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU D 425 |
| Chain | Residue |
| C | ARG135 |
| D | ALA73 |
| D | ARG420 |
| D | GLY421 |
| D | LEU422 |
| D | TYR423 |
| D | HOH447 |
| D | HOH591 |
| F | ASP167 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU E 500 |
| Chain | Residue |
| E | GLY79 |
| E | GLY80 |
| E | MET99 |
| E | LYS114 |
| E | PRO153 |
| E | ASP154 |
| E | VAL354 |
| E | SER357 |
| E | HOH1522 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU E 425 |
| Chain | Residue |
| E | HOH1363 |
| F | ARG135 |
| C | ASP167 |
| C | MET171 |
| E | ALA73 |
| E | ARG420 |
| E | GLY421 |
| E | LEU422 |
| E | TYR423 |
| E | HOH846 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLU F 500 |
| Chain | Residue |
| F | GLY80 |
| F | MET99 |
| F | LYS114 |
| F | ALA152 |
| F | PRO153 |
| F | ASP154 |
| F | ARG194 |
| F | VAL354 |
| F | SER357 |
| F | HOH979 |
| F | HOH1542 |
| F | HOH1798 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLU F 425 |
| Chain | Residue |
| B | ASP167 |
| B | MET171 |
| E | ARG135 |
| F | ALA73 |
| F | ARG417 |
| F | ARG420 |
| F | GLY421 |
| F | LEU422 |
| F | TYR423 |
| F | HOH432 |
| F | HOH445 |
| F | HOH961 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU G 500 |
| Chain | Residue |
| G | GLY80 |
| G | MET99 |
| G | LYS114 |
| G | ALA152 |
| G | PRO153 |
| G | ASP154 |
| G | ARG194 |
| G | SER357 |
| G | HOH471 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GLU G 425 |
| Chain | Residue |
| G | ALA73 |
| G | ARG417 |
| G | ARG420 |
| G | GLY421 |
| G | LEU422 |
| G | TYR423 |
| G | HOH474 |
| G | HOH881 |
| I | ASP167 |
| I | MET171 |
| J | ARG135 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU H 500 |
| Chain | Residue |
| H | GLY80 |
| H | MET99 |
| H | LYS114 |
| H | ALA152 |
| H | PRO153 |
| H | ASP154 |
| H | ARG194 |
| H | SER357 |
| H | HOH1156 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU H 425 |
| Chain | Residue |
| G | ASP167 |
| G | MET171 |
| H | ARG417 |
| H | ARG420 |
| H | GLY421 |
| H | LEU422 |
| H | TYR423 |
| H | HOH446 |
| L | ARG135 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLU I 500 |
| Chain | Residue |
| I | GLY80 |
| I | MET99 |
| I | LYS114 |
| I | PRO153 |
| I | ASP154 |
| I | ARG194 |
| I | SER357 |
| I | HOH453 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU I 425 |
| Chain | Residue |
| H | ASP167 |
| I | THR72 |
| I | ALA73 |
| I | ARG420 |
| I | GLY421 |
| I | LEU422 |
| I | TYR423 |
| I | HOH451 |
| I | HOH632 |
| K | ARG135 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU J 500 |
| Chain | Residue |
| J | GLY79 |
| J | GLY80 |
| J | MET99 |
| J | LYS114 |
| J | ALA152 |
| J | PRO153 |
| J | ASP154 |
| J | VAL354 |
| J | SER357 |
| J | HOH1720 |
| site_id | CC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLU J 425 |
| Chain | Residue |
| G | ARG135 |
| J | LYS44 |
| J | ALA73 |
| J | ARG417 |
| J | ARG420 |
| J | GLY421 |
| J | LEU422 |
| J | TYR423 |
| J | HOH1124 |
| J | HOH1420 |
| L | ASP167 |
| L | MET171 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLU K 500 |
| Chain | Residue |
| K | GLY80 |
| K | MET99 |
| K | LYS114 |
| K | PRO153 |
| K | ASP154 |
| K | ARG194 |
| K | GLY353 |
| K | SER357 |
| site_id | CC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GLU K 425 |
| Chain | Residue |
| I | ARG135 |
| J | ASP167 |
| K | ALA73 |
| K | ARG417 |
| K | ARG420 |
| K | GLY421 |
| K | LEU422 |
| K | TYR423 |
| K | HOH436 |
| K | HOH446 |
| K | HOH1310 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU L 500 |
| Chain | Residue |
| L | GLY80 |
| L | MET99 |
| L | LYS114 |
| L | PRO153 |
| L | ASP154 |
| L | ARG194 |
| L | GLY353 |
| L | SER357 |
| L | HOH433 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU L 425 |
| Chain | Residue |
| H | ARG135 |
| K | ASP167 |
| K | MET171 |
| L | ALA73 |
| L | ARG420 |
| L | GLY421 |
| L | LEU422 |
| L | TYR423 |
| L | HOH1112 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 426 |
| Chain | Residue |
| A | TYR368 |
| A | GLU374 |
| A | HOH1697 |
| C | ARG378 |
| C | ARG381 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NH4 A 427 |
| Chain | Residue |
| A | ARG381 |
| A | HOH433 |
| A | HOH1369 |
| E | TYR368 |
| E | GLU374 |
| site_id | CC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NH4 B 426 |
| Chain | Residue |
| B | HOH434 |
| B | HOH449 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 426 |
| Chain | Residue |
| C | TYR368 |
| C | GLU374 |
| E | ARG378 |
| E | ARG381 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 426 |
| Chain | Residue |
| B | ARG378 |
| B | ARG381 |
| D | TYR368 |
| D | GLU374 |
| D | HOH941 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 F 426 |
| Chain | Residue |
| B | TYR368 |
| B | GLU374 |
| F | ARG378 |
| F | ARG381 |
| F | HOH1407 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NH4 F 427 |
| Chain | Residue |
| F | HIS241 |
| F | GLU380 |
| F | HOH493 |
| site_id | DC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 G 426 |
| Chain | Residue |
| G | TYR368 |
| G | GLU374 |
| G | HOH427 |
| G | HOH928 |
| H | ARG378 |
| H | ARG381 |
| site_id | DC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NH4 H 426 |
| Chain | Residue |
| H | LYS114 |
| H | ASP154 |
| H | HOH441 |
| site_id | DC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 I 426 |
| Chain | Residue |
| G | ARG378 |
| G | ARG381 |
| G | HOH1343 |
| I | TYR368 |
| I | GLU374 |
| I | HOH449 |
| I | HOH966 |
| site_id | DC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 I 427 |
| Chain | Residue |
| H | TYR368 |
| H | GLU374 |
| I | ARG378 |
| I | ARG381 |
| site_id | DC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 J 426 |
| Chain | Residue |
| J | ARG378 |
| J | ARG381 |
| J | HOH653 |
| L | TYR368 |
| L | GLU374 |
| site_id | EC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NH4 J 427 |
| Chain | Residue |
| J | HIS241 |
| J | GLU380 |
| J | HOH1221 |
| site_id | EC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 K 426 |
| Chain | Residue |
| K | TYR368 |
| K | GLU374 |
| L | ARG378 |
| L | ARG381 |
| site_id | EC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NH4 L 426 |
| Chain | Residue |
| L | LEU192 |
| L | GLY193 |
| L | GLU372 |
| L | HOH432 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGirvDP |
| Chain | Residue | Details |
| A | LEU108-PRO121 |
