1K75
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
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 | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 0008652 | biological_process | amino acid biosynthetic process |
| 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 | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
| Chain | Residue |
| A | PRO236 |
| A | HOH2425 |
| A | SER237 |
| A | HIS262 |
| A | GLY263 |
| A | PRO264 |
| A | ASP265 |
| A | SER266 |
| A | HOH2075 |
| A | HOH2156 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
| Chain | Residue |
| B | PRO236 |
| B | SER237 |
| B | HIS262 |
| B | GLY263 |
| B | PRO264 |
| B | ASP265 |
| B | SER266 |
| B | HOH2119 |
| B | HOH2287 |
| B | HOH2397 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2003 |
| Chain | Residue |
| B | PRO249 |
| B | ARG280 |
| B | HOH2010 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2004 |
| Chain | Residue |
| A | PRO249 |
| A | ARG280 |
| A | HOH2051 |
| B | ARG287 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1001 |
| Chain | Residue |
| A | GLU72 |
| A | ILE165 |
| A | ASN183 |
| A | HOH2118 |
| A | HOH2268 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11842181","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11842181","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11842181","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 741 |
| Chain | Residue | Details |
| A | ALA275 | metal ligand |
| A | ALA278 | metal ligand |
| A | GLY346 | proton acceptor, proton donor |
| A | SER347 | proton acceptor, proton donor |
| A | SER380 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 741 |
| Chain | Residue | Details |
| B | ALA275 | metal ligand |
| B | ALA278 | metal ligand |
| B | GLY346 | proton acceptor, proton donor |
| B | SER347 | proton acceptor, proton donor |
| B | SER380 | metal ligand |
