› 4g07

X-ray diffraction
1.95Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 47.18 KDa
Source organism: Brucella suis 1330
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8G2R2 (Residues: 1-430; Coverage: 100%)
Gene names: BR0252, BS1330_I0253, hisD
Sequence domains: Histidinol dehydrogenase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 76.672Å b: 105.075Å c: 112.416Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.239
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX.
Langella et al. (2018)
3 more

2 mentions without citation

The Role of Gene Elongation in the Evolution of Histidine Biosynthetic Genes.
Del Duca et al. (2020)
1 more