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Structure paper

TitlePartial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations.
Journal, issue, pagesBiochemistry, Vol. 60, Page 2309-2319, Year 2021
Publish dateApr 27, 2021 (structure data deposition date)
AuthorsKozuka, K. / Nakano, S. / Asano, Y. / Ito, S.
External linksBiochemistry / PubMed:34254784
MethodsX-ray diffraction
Resolution2.102 - 2.2 Å
Structure data

PDB-7epr:
Partial Consensus L-threonine 3-dehydrogenase (C-Change)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-7eps:
Partial Consensus L-threonine 3-dehydrogenase (E-change)
Method: X-RAY DIFFRACTION / Resolution: 2.102 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-THR:
THREONINE

ChemComp-PE4:
2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / precipitant*YM

Source
  • synthetic construct (others)
KeywordsOXIDOREDUCTASE / L-threonine 3-dehydrogenase / artificial protein

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