› 1kae

X-ray diffraction
1.7Å resolution

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

Released:
DOI: 10.2210/pdb1kae/pdb
PDB entry 1kae coloured by chain, front view.
PDB entry 1kae coloured by chain, side view.
PDB entry 1kae coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase.
Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M
Proc Natl Acad Sci U S A 99 1859-64 (2002)
PMID: 11842181

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139324 (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:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
6 bound ligands:
Ligand SO4 4 x SO4
Ligand ZN 2 x ZN
Ligand DTT 1 x DTT
Ligand HSO 1 x HSO
Ligand IMD 1 x IMD
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 14 x MSE

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

Quick links

Citations

1 review citation

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.
Kulis-Horn et al. (2014)
19 other articles

8 mentions without citation

Contribution of structural genomics to understanding the biology of Escherichia coli.
Matte et al. (2003)
7 more