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TitleIn silico enzyme screening identifies an SDR ketoreductase from Thermus caliditerrae as an attractive biocatalyst and promising candidate for protein engineering
Journal, issue, pagesFront Chem Biol, Year 2024
Publish dateMay 17, 2024 (structure data deposition date)
AuthorsSosa, Y. / Kapur, B. / Hurtak, J. / Kingsley, L. / Wu, H. / Gruber, S. / Nar, H. / Khattabi, S. / Moral, J. / Lucas, M. ...Sosa, Y. / Kapur, B. / Hurtak, J. / Kingsley, L. / Wu, H. / Gruber, S. / Nar, H. / Khattabi, S. / Moral, J. / Lucas, M. / Martin, C. / Loncar, N. / Buono, F. / Pefaur, N. / Nixon, A.E. / Song, J.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.698 - 1.875 Å
Structure data

PDB-9fe6:
Short-chain dehydrogenase/reductase (SDR) from Thermus caliditerrae
Method: X-RAY DIFFRACTION / Resolution: 1.875 Å

PDB-9feb:
Short-chain dehydrogenase/reductase (SDR) from Thermus caliditerrae in complex with NADP
Method: X-RAY DIFFRACTION / Resolution: 1.698 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Source
  • thermus caliditerrae (bacteria)
KeywordsOXIDOREDUCTASE / short chain dehydrogenase / ketoreductase / biocatalysis

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