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TitleBinding of NAD+ and L-Threonine Induces Stepwise Structural and Flexibility Changes in Cupriavidus necator L-Threonine Dehydrogenase
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 10445-10454, Year 2014
Publish dateNov 29, 2013 (structure data deposition date)
AuthorsNakano, S. / Okazaki, S. / Tokiwa, H. / Asano, Y.
External linksJ. Biol. Chem. / PubMed:24558034
MethodsX-ray diffraction
Resolution2.25 - 2.5 Å
Structure data

PDB-3wmw:
GalE-like L-Threonine dehydrogenase from Cupriavidus necator (apo form)
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-3wmx:
GalE-like L-Threonine dehydrogenase from Cupriavidus necator (holo form)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-THR:
THREONINE

Source
  • ralstonia eutropha (bacteria)
KeywordsOXIDOREDUCTASE / Rossmann Fold / dehydrogenase / NAD+ binding / extended short-chain dehydrogenase/reductase superfamily

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