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 | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 | 0030145 | molecular_function | manganese ion binding |
| 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 | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| 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 | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 701 |
| Chain | Residue |
| A | PRO293 |
| A | LYS420 |
| A | HOH1267 |
| A | HOH1351 |
| B | ARG415 |
| B | THR417 |
| B | HOH1231 |
| B | HOH1254 |
| B | HOH1326 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 702 |
| Chain | Residue |
| A | SER81 |
| A | ASP82 |
| A | HOH1343 |
| A | HOH1352 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 703 |
| Chain | Residue |
| B | PRO249 |
| B | ARG280 |
| B | HOH1238 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 704 |
| Chain | Residue |
| A | PRO249 |
| A | ARG280 |
| A | HOH1231 |
| B | ARG287 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1101 |
| Chain | Residue |
| A | GLN259 |
| A | HIS262 |
| A | ASP360 |
| A | HSO1001 |
| B | HIS419 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1102 |
| Chain | Residue |
| A | HIS419 |
| B | HIS262 |
| B | ASP360 |
| B | IMD902 |
| B | HOH1299 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DTT A 901 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IMD B 902 |
| Chain | Residue |
| A | GLU414 |
| A | LEU416 |
| A | HIS419 |
| B | SER140 |
| B | HIS262 |
| B | ASP360 |
| B | TYR361 |
| B | HIS367 |
| B | ZN1102 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HSO A 1001 |
| Chain | Residue |
| A | SER140 |
| A | SER237 |
| A | GLN259 |
| A | HIS262 |
| A | HIS327 |
| A | GLU356 |
| A | ASP360 |
| A | TYR361 |
| A | HIS367 |
| A | ZN1101 |
| B | GLU414 |
| B | LEU416 |
| B | HIS419 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAD A 1201 |
| Chain | Residue |
| A | PHE58 |
| A | TYR130 |
| A | PRO132 |
| A | PRO162 |
| A | GLY186 |
| A | GLN188 |
| A | GLY210 |
| A | ASN211 |
| A | PHE213 |
| A | VAL214 |
| A | HOH1426 |
| A | HOH1440 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NAD B 1202 |
| Chain | Residue |
| B | TYR130 |
| B | PRO132 |
| B | GLY133 |
| B | PRO162 |
| B | ASN211 |
| B | VAL214 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 801 |
| Chain | Residue |
| B | PRO273 |
| B | ASP312 |
| B | LEU313 |
| B | HOH1272 |
| B | HOH1290 |
Functional Information from PROSITE/UniProt
| site_id | PS00611 |
| Number of Residues | 33 |
| Details | HISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmp.AGPSEVLVIAdsgAtpdf..VASDLLSqaEH |
| Chain | Residue | Details |
| A | ILE230-HIS262 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS327 | |
| A | LEU328 | |
| B | HIS327 | |
| B | LEU328 | |
| Chain | Residue | Details |
| A | ILE131 | |
| B | ALA212 | |
| B | ALA260 | |
| B | GLY263 | |
| B | TYR361 | |
| B | LYS420 | |
| A | ALA189 | |
| A | ALA212 | |
| A | ALA260 | |
| A | GLY263 | |
| A | TYR361 | |
| A | LYS420 | |
| B | ILE131 | |
| B | ALA189 | |
| Chain | Residue | Details |
| A | GLU238 | |
| A | LEU328 | |
| A | ARG415 | |
| B | GLU238 | |
| B | LEU328 | |
| B | ARG415 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11842181 |
| Chain | Residue | Details |
| A | GLU326 | |
| A | HIS327 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11842181 |
| Chain | Residue | Details |
| B | GLU326 | |
| B | HIS327 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 741 |
| Chain | Residue | Details |
| A | ALA260 | metal ligand |
| A | GLY263 | metal ligand |
| A | HIS327 | proton acceptor, proton donor |
| A | LEU328 | proton acceptor, proton donor |
| A | TYR361 | metal ligand |
| A | LYS420 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 741 |
| Chain | Residue | Details |
| B | ALA260 | metal ligand |
| B | GLY263 | metal ligand |
| B | HIS327 | proton acceptor, proton donor |
| B | LEU328 | proton acceptor, proton donor |
| B | TYR361 | metal ligand |
| B | LYS420 | metal ligand |
