5VLD
Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004399 | molecular_function | histidinol dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0004399 | molecular_function | histidinol dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0004399 | molecular_function | histidinol dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0000166 | molecular_function | nucleotide binding |
| D | 0004399 | molecular_function | histidinol dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0000166 | molecular_function | nucleotide binding |
| E | 0004399 | molecular_function | histidinol dehydrogenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0000166 | molecular_function | nucleotide binding |
| F | 0004399 | molecular_function | histidinol dehydrogenase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 15 |
| Details | binding site for residue HIS A 501 |
| Chain | Residue |
| A | LEU174 |
| A | TYR402 |
| A | HIS408 |
| A | NAD502 |
| B | GLU455 |
| B | HIS460 |
| B | ZN501 |
| A | SER176 |
| A | SER277 |
| A | GLN299 |
| A | HIS302 |
| A | GLU367 |
| A | HIS368 |
| A | GLU397 |
| A | ASP401 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue NAD A 502 |
| Chain | Residue |
| A | PHE96 |
| A | ASP97 |
| A | TYR166 |
| A | PRO168 |
| A | GLY169 |
| A | GLY170 |
| A | THR171 |
| A | PRO198 |
| A | GLY225 |
| A | GLY226 |
| A | GLN228 |
| A | PRO249 |
| A | GLY250 |
| A | ASN251 |
| A | TYR253 |
| A | ALA274 |
| A | GLY275 |
| A | PRO276 |
| A | SER277 |
| A | HIS302 |
| A | GLU367 |
| A | HIS408 |
| A | VAL409 |
| A | LEU410 |
| A | THR412 |
| A | HIS501 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 503 |
| Chain | Residue |
| A | HIS460 |
| B | GLN299 |
| B | HIS302 |
| B | ASP401 |
| B | HIS502 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 504 |
| Chain | Residue |
| A | GLN91 |
| A | TYR92 |
| A | LYS95 |
| E | LYS285 |
| E | GLY316 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| A | GLN299 |
| A | HIS302 |
| A | ASP401 |
| A | HIS501 |
| B | HIS460 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue HIS B 502 |
| Chain | Residue |
| A | GLU455 |
| A | LEU457 |
| A | HIS460 |
| A | ZN503 |
| B | LEU174 |
| B | SER176 |
| B | SER277 |
| B | GLN299 |
| B | HIS302 |
| B | GLU367 |
| B | HIS368 |
| B | GLU397 |
| B | ASP401 |
| B | TYR402 |
| B | HIS408 |
| B | NAD503 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | binding site for residue NAD B 503 |
| Chain | Residue |
| B | HOH606 |
| B | PHE96 |
| B | ASP97 |
| B | TYR166 |
| B | PRO168 |
| B | GLY169 |
| B | GLY170 |
| B | THR171 |
| B | PRO198 |
| B | GLY225 |
| B | GLY226 |
| B | GLN228 |
| B | PRO249 |
| B | GLY250 |
| B | ASN251 |
| B | TYR253 |
| B | VAL254 |
| B | ALA274 |
| B | GLY275 |
| B | PRO276 |
| B | SER277 |
| B | HIS302 |
| B | GLU367 |
| B | HIS408 |
| B | VAL409 |
| B | LEU410 |
| B | THR412 |
| B | HIS502 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | GLN299 |
| C | HIS302 |
| C | ASP401 |
| C | HIS502 |
| D | HIS460 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue HIS 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 |
| C | NAD503 |
| D | GLU455 |
| D | LEU457 |
| D | HIS460 |
| site_id | AD1 |
| Number of Residues | 26 |
| Details | binding site for residue NAD C 503 |
| Chain | Residue |
| C | PHE96 |
| C | ASP97 |
| C | TYR166 |
| C | PRO168 |
| C | GLY169 |
| C | GLY170 |
| C | THR171 |
| C | PRO198 |
| C | GLY225 |
| C | GLN228 |
| C | PRO249 |
| C | GLY250 |
| C | ASN251 |
| C | TYR253 |
| C | VAL254 |
| C | ALA274 |
| C | GLY275 |
| C | PRO276 |
| C | SER277 |
| C | HIS302 |
| C | GLU367 |
| C | HIS408 |
| C | VAL409 |
| C | LEU410 |
| C | THR412 |
| C | HIS502 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| C | HIS460 |
| D | GLN299 |
| D | HIS302 |
| D | ASP401 |
| D | HIS502 |
| site_id | AD3 |
| Number of Residues | 16 |
| Details | binding site for residue HIS D 502 |
| Chain | Residue |
| C | GLU455 |
| C | LEU457 |
| C | HIS460 |
| D | LEU174 |
| D | SER176 |
| D | SER277 |
| D | GLN299 |
| D | HIS302 |
| D | GLU367 |
| D | HIS368 |
| D | GLU397 |
| D | ASP401 |
| D | TYR402 |
| D | HIS408 |
| D | ZN501 |
| D | NAD503 |
| site_id | AD4 |
| Number of Residues | 25 |
| Details | binding site for residue NAD D 503 |
| Chain | Residue |
| D | PHE96 |
| D | ASP97 |
| D | TYR166 |
| D | PRO168 |
| D | GLY169 |
| D | GLY170 |
| D | THR171 |
| D | ALA172 |
| D | PRO198 |
| D | GLN228 |
| D | PRO249 |
| D | GLY250 |
| D | ASN251 |
| D | TYR253 |
| D | ALA274 |
| D | GLY275 |
| D | PRO276 |
| D | SER277 |
| D | HIS302 |
| D | GLU367 |
| D | HIS408 |
| D | VAL409 |
| D | LEU410 |
| D | THR412 |
| D | HIS502 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN E 501 |
| Chain | Residue |
| E | GLN299 |
| E | HIS302 |
| E | ASP401 |
| E | HIS502 |
| F | HIS460 |
| site_id | AD6 |
| Number of Residues | 14 |
| Details | binding site for residue HIS E 502 |
| Chain | Residue |
| E | SER176 |
| E | SER277 |
| E | GLN299 |
| E | HIS302 |
| E | GLU367 |
| E | HIS368 |
| E | GLU397 |
| E | ASP401 |
| E | TYR402 |
| E | HIS408 |
| E | ZN501 |
| E | NAD503 |
| F | GLU455 |
| F | HIS460 |
| site_id | AD7 |
| Number of Residues | 26 |
| Details | binding site for residue NAD E 503 |
| Chain | Residue |
| E | PHE96 |
| E | ASP97 |
| E | TYR166 |
| E | PRO168 |
| E | GLY169 |
| E | GLY170 |
| E | THR171 |
| E | PRO198 |
| E | GLN228 |
| E | PRO249 |
| E | GLY250 |
| E | ASN251 |
| E | TYR253 |
| E | VAL254 |
| E | ALA274 |
| E | GLY275 |
| E | PRO276 |
| E | SER277 |
| E | HIS302 |
| E | GLU367 |
| E | HIS408 |
| E | VAL409 |
| E | LEU410 |
| E | THR412 |
| E | HIS502 |
| E | HOH607 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN E 504 |
| Chain | Residue |
| E | HIS460 |
| F | GLN299 |
| F | HIS302 |
| F | ASP401 |
| F | HIS501 |
| site_id | AD9 |
| Number of Residues | 15 |
| Details | binding site for residue HIS F 501 |
| Chain | Residue |
| E | GLU455 |
| E | HIS460 |
| E | ZN504 |
| F | LEU174 |
| F | SER176 |
| F | SER277 |
| F | GLN299 |
| F | HIS302 |
| F | GLU367 |
| F | HIS368 |
| F | GLU397 |
| F | ASP401 |
| F | TYR402 |
| F | HIS408 |
| F | NAD502 |
| site_id | AE1 |
| Number of Residues | 28 |
| Details | binding site for residue NAD F 502 |
| Chain | Residue |
| B | ASN320 |
| F | PHE96 |
| F | ASP97 |
| F | TYR166 |
| F | PRO168 |
| F | GLY169 |
| F | GLY170 |
| F | THR171 |
| F | PRO198 |
| F | GLY225 |
| F | GLY226 |
| F | GLN228 |
| F | PRO249 |
| F | GLY250 |
| F | ASN251 |
| F | TYR253 |
| F | VAL254 |
| F | ALA274 |
| F | GLY275 |
| F | PRO276 |
| F | SER277 |
| F | HIS302 |
| F | GLU367 |
| F | HIS408 |
| F | VAL409 |
| F | LEU410 |
| F | THR412 |
| F | HIS501 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue PEG F 503 |
| Chain | Residue |
| E | HOH628 |
| F | MET363 |
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 |
