1KAR
L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH HISTAMINE (INHIBITOR), ZINC AND NAD (COFACTOR)
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS262 |
| A | ASP360 |
| A | HSM502 |
| B | HIS419 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| A | HIS419 |
| B | HIS262 |
| B | ASP360 |
| B | HSM503 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HSM A 502 |
| Chain | Residue |
| A | HIS262 |
| A | ASP360 |
| A | TYR361 |
| A | HIS367 |
| A | ZN501 |
| B | GLU414 |
| B | LEU416 |
| B | HIS419 |
| A | SER140 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HSM B 503 |
| Chain | Residue |
| A | GLU414 |
| A | HIS419 |
| B | SER140 |
| B | HIS262 |
| B | ASP360 |
| B | TYR361 |
| B | HIS367 |
| B | ZN502 |
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 | ARG279 | metal ligand |
| A | ALA282 | metal ligand |
| A | LEU350 | proton acceptor, proton donor |
| A | GLY351 | proton acceptor, proton donor |
| A | ALA384 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 741 |
| Chain | Residue | Details |
| B | ARG279 | metal ligand |
| B | ALA282 | metal ligand |
| B | LEU350 | proton acceptor, proton donor |
| B | GLY351 | proton acceptor, proton donor |
| B | ALA384 | metal ligand |
