5VLC
Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004399 | molecular_function | histidinol dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004399 | molecular_function | histidinol dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009507 | cellular_component | chloroplast |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0004399 | molecular_function | histidinol dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009507 | cellular_component | chloroplast |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0004399 | molecular_function | histidinol dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009507 | cellular_component | chloroplast |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
| E | 0000105 | biological_process | L-histidine biosynthetic process |
| E | 0004399 | molecular_function | histidinol dehydrogenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009507 | cellular_component | chloroplast |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051287 | molecular_function | NAD binding |
| F | 0000105 | biological_process | L-histidine biosynthetic process |
| F | 0004399 | molecular_function | histidinol dehydrogenase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009507 | cellular_component | chloroplast |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue HSO A 501 |
| Chain | Residue |
| A | SER176 |
| B | GLU455 |
| B | LEU457 |
| B | HIS460 |
| B | ZN501 |
| A | GLN299 |
| A | HIS302 |
| A | GLU367 |
| A | HIS368 |
| A | GLU397 |
| A | ASP401 |
| A | TYR402 |
| A | HIS408 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | HIS460 |
| B | GLN299 |
| B | HIS302 |
| B | ASP401 |
| B | HSO502 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| A | GLN299 |
| A | HIS302 |
| A | ASP401 |
| A | HSO501 |
| B | HIS460 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue HSO B 502 |
| Chain | Residue |
| A | GLU455 |
| A | LEU457 |
| A | HIS460 |
| A | ZN502 |
| B | LEU174 |
| B | SER176 |
| B | SER277 |
| B | GLN299 |
| B | HIS302 |
| B | GLU367 |
| B | HIS368 |
| B | GLU397 |
| B | ASP401 |
| B | TYR402 |
| B | HIS408 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | GLN299 |
| C | HIS302 |
| C | ASP401 |
| C | HSO502 |
| D | HIS460 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue HSO C 502 |
| Chain | Residue |
| C | SER176 |
| C | SER277 |
| C | GLN299 |
| C | HIS302 |
| C | GLU367 |
| C | HIS368 |
| C | GLU397 |
| C | ASP401 |
| C | TYR402 |
| C | HIS408 |
| C | ZN501 |
| D | GLU455 |
| D | LEU457 |
| D | HIS460 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| C | HIS460 |
| D | GLN299 |
| D | HIS302 |
| D | ASP401 |
| D | HSO502 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue HSO D 502 |
| Chain | Residue |
| C | GLU455 |
| C | LEU457 |
| C | HIS460 |
| D | SER176 |
| D | SER277 |
| D | GLN299 |
| D | HIS302 |
| D | GLU367 |
| D | HIS368 |
| D | GLU397 |
| D | ASP401 |
| D | TYR402 |
| D | HIS408 |
| D | ZN501 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN E 501 |
| Chain | Residue |
| E | GLN299 |
| E | HIS302 |
| E | ASP401 |
| E | HSO502 |
| F | HIS460 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue HSO E 502 |
| Chain | Residue |
| E | SER176 |
| E | GLN299 |
| E | HIS302 |
| E | GLU367 |
| E | HIS368 |
| E | GLU397 |
| E | ASP401 |
| E | TYR402 |
| E | HIS408 |
| E | ZN501 |
| F | GLU455 |
| F | LEU457 |
| F | HIS460 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN E 503 |
| Chain | Residue |
| E | HIS460 |
| F | GLN299 |
| F | HIS302 |
| F | ASP401 |
| F | HSO501 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue HSO F 501 |
| Chain | Residue |
| E | GLU455 |
| E | LEU457 |
| E | HIS460 |
| E | ZN503 |
| F | LEU174 |
| F | SER176 |
| F | SER277 |
| F | GLN299 |
| F | HIS302 |
| F | GLU367 |
| F | HIS368 |
| F | GLU397 |
| F | ASP401 |
| F | TYR402 |
| F | HIS408 |
Functional Information from PROSITE/UniProt
| site_id | PS00611 |
| Number of Residues | 33 |
| Details | HISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmp.AGPSEVLVIAdkhAipsh..VAADLLSqaEH |
| Chain | Residue | Details |
| A | ILE270-HIS302 |
