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Structure paper

TitleProtein Sequence Selection Method That Enables Full Consensus Design of Artificial l-Threonine 3-Dehydrogenases with Unique Enzymatic Properties.
Journal, issue, pagesBiochemistry, Vol. 59, Page 3823-3833, Year 2020
Publish dateJul 2, 2020 (structure data deposition date)
AuthorsMotoyama, T. / Hiramatsu, N. / Asano, Y. / Nakano, S. / Ito, S.
External linksBiochemistry / PubMed:32945652
MethodsX-ray diffraction
Resolution2.38 Å
Structure data

PDB-7cgv:
Full consensus L-threonine 3-dehydrogenase, FcTDH-IIYM (NAD+ bound form)
Method: X-RAY DIFFRACTION / Resolution: 2.38 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • synthetic construct (others)
KeywordsOXIDOREDUCTASE / L-Threonine 3-dehydrogenase / Artificial protein / Full consensus design

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