PDBe 1kae

X-ray diffraction
1.7Å resolution

L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINOL (SUBSTRATE), ZINC AND NAD (COFACTOR)

Released:

Function and Biology Details

Reaction catalysed:
L-histidinol + H(2)O + 2 NAD(+) = L-histidine + 2 NADH. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 434 amino acids
Theoretical weight: 46.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06988 (Residues: 1-434; Coverage: 100%)
Gene names: JW2002, b2020, hisD
Sequence domains: Histidinol dehydrogenase
Structure domains: Nitrogenase molybdenum iron protein domain

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P212121
Unit cell:
a: 54.93Å b: 107.94Å c: 156.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.241
Expression system: Escherichia coli