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 |