› 2dfv

X-ray diffraction
2.05Å resolution

Hyperthermophilic threonine dehydrogenase from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb2dfv/pdb
PDB entry 2dfv coloured by chain, front view.
PDB entry 2dfv coloured by chain, side view.
PDB entry 2dfv coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
The first crystal structure of L-threonine dehydrogenase.
Ishikawa K, Higashi N, Nakamura T, Matsuura T, Nakagawa A
J Mol Biol 366 857-67 (2007)
PMID: 17188300

Function and Biology Details

Reaction catalysed: 
L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-threonine 3-dehydrogenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 347 amino acids
Theoretical weight: 37.98 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58389 (Residues: 2-348; Coverage: 100%)
Gene names: PH0655, tdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 3 x NAD
2 bound ligands:
Ligand ZN 3 x ZN
Ligand SO4 3 x SO4
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: I4122
Unit cell:
a: 144.433Å b: 144.433Å c: 305.069Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.239
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The mismetallation of enzymes during oxidative stress.
Imlay JA. (2014)
2 more

1 mention without citation

Substitutions at the cofactor phosphate-binding site of a clostridial alcohol dehydrogenase lead to unexpected changes in substrate specificity.
Maddock et al. (2015)