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X-ray diffraction
2.4Å resolution

L-Threonine Dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Released:
DOI: 10.2210/pdb3gfb/pdb
PDB entry 3gfb coloured by chain, front view.
PDB entry 3gfb coloured by chain, side view.
PDB entry 3gfb coloured by chain, top view.
Source organism: Thermococcus kodakarensis KOD1
Primary publication:
Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis.
Bowyer A, Mikolajek H, Stuart JW, Wood SP, Jamil F, Rashid N, Akhtar M, Cooper JB
J Struct Biol 168 294-304 (2009)
PMID: 19616102

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:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-threonine 3-dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 350 amino acids
Theoretical weight: 38.15 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5JI69 (Residues: 1-350; Coverage: 100%)
Gene names: TK0916, tdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P43212
Unit cell:
a: 124.481Å b: 124.481Å c: 271.143Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.277
Expression system: Escherichia coli

Quick links

Citations

1 review citation

An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.
Rashid et al. (2020)
14 other articles

3 mentions without citation

Molecular characterization of an NADPH-dependent acetoin reductase/2,3-butanediol dehydrogenase from Clostridium beijerinckii NCIMB 8052.
Raedts et al. (2014)
2 more