› 2yy7

X-ray diffraction
2.06Å resolution

Crystal structure of thermolabile L-threonine dehydrogenase from Flavobacterium frigidimaris KUC-1

Released:
DOI: 10.2210/pdb2yy7/pdb
PDB entry 2yy7 coloured by chain, front view.
PDB entry 2yy7 coloured by chain, side view.
PDB entry 2yy7 coloured by chain, top view.
Source organism: Flavobacterium frigidimaris
Primary publication:
Crystal structure of UDP-galactose 4-epimerase-like L-threonine dehydrogenase belonging to the intermediate short-chain dehydrogenase-reductase superfamily.
Yoneda K, Sakuraba H, Muraoka I, Oikawa T, Ohshima T
FEBS J 277 5124-32 (2010)
PMID: 21078123

Function and Biology Details

Reaction catalysed: 
L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185227 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent epimerase/dehydratase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 35.45 KDa
Source organism: Flavobacterium frigidimaris
UniProt:
  • Canonical: Q8KZM4 (Residues: 1-312; Coverage: 100%)
Gene name: ltd
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
3 bound ligands:
Ligand PE8 4 x PE8
Ligand MES 2 x MES
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 61.029Å b: 88.142Å c: 123.944Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.203

Quick links

Citations

1 review citation

Enzymes from Marine Polar Regions and Their Biotechnological Applications.
Bruno et al. (2019)
10 other articles

3 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
2 more