› 5vlc

X-ray diffraction
1.97Å resolution

Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol

Released:
DOI: 10.2210/pdb5vlc/pdb
PDB entry 5vlc coloured by chain, front view.
PDB entry 5vlc coloured by chain, side view.
PDB entry 5vlc coloured by chain, top view.
Source organism: Medicago truncatula
Primary publication:
Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD+ Binding and the Cofactor Positioned to Accept a Hydride.
Ruszkowski M, Dauter Z
OpenAccess logo Sci Rep 7 10476 (2017)
PMID: 28874718

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-515534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol dehydrogenase, chloroplastic Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 446 amino acids
Theoretical weight: 48.19 KDa
Source organism: Medicago truncatula
Expression system: Escherichia coli
UniProt:
  • Canonical: G7IKX3 (Residues: 36-478; Coverage: 93%)
Gene names: 11412251, MTR_2g030520, MtrunA17_Chr2g0292691
Sequence domains: Histidinol dehydrogenase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand HSO 6 x HSO
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 102.859Å b: 139.201Å c: 102.692Å
α: 90° β: 119.18° γ: 90°
R-values:
R R work R free
0.179 0.179 0.229
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Chloroplastic Serine Hydroxymethyltransferase From Medicago truncatula: A Structural Characterization.
Ruszkowski 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