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Structure paper

TitleOrigins of stereoselectivity in evolved ketoreductases.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 112, Page E7065-E7072, Year 2015
Publish dateSep 24, 2014 (structure data deposition date)
AuthorsNoey, E.L. / Tibrewal, N. / Jimenez-Oses, G. / Osuna, S. / Park, J. / Bond, C.M. / Cascio, D. / Liang, J. / Zhang, X. / Huisman, G.W. ...Noey, E.L. / Tibrewal, N. / Jimenez-Oses, G. / Osuna, S. / Park, J. / Bond, C.M. / Cascio, D. / Liang, J. / Zhang, X. / Huisman, G.W. / Tang, Y. / Houk, K.N.
External linksProc. Natl. Acad. Sci. USA / PubMed:26644568
MethodsX-ray diffraction
Resolution1.596 - 2.201 Å
Structure data

PDB-4rf2:
Crystal structure of NADP+ bound ketoreductase from Lactobacillus kefir
Method: X-RAY DIFFRACTION / Resolution: 2.089 Å

PDB-4rf3:
Crystal Structure of ketoreductase from Lactobacillus kefir, mutant A94F
Method: X-RAY DIFFRACTION / Resolution: 1.694 Å

PDB-4rf4:
Crystal structure of ketoreductase from Lactobacillus kefir
Method: X-RAY DIFFRACTION / Resolution: 2.201 Å

PDB-4rf5:
Crystal structure of ketoreductase from Lactobacillus kefir, E145S mutant
Method: X-RAY DIFFRACTION / Resolution: 1.596 Å

Chemicals

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • lactobacillus kefiri (bacteria)
KeywordsOXIDOREDUCTASE

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