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Structure paper

TitleMutational and structural studies uncover crucial amino acids determining activity and stability of 17 beta-HSD14.
Journal, issue, pagesJ. Steroid Biochem. Mol. Biol., Vol. 189, Page 135-144, Year 2019
Publish dateJan 5, 2018 (structure data deposition date)
AuthorsBadran, M.J. / Bertoletti, N. / Keils, A. / Heine, A. / Klebe, G. / Marchais-Oberwinkler, S.
External linksJ. Steroid Biochem. Mol. Biol. / PubMed:30836176
MethodsX-ray diffraction
Resolution1.65 - 1.68 Å
Structure data

PDB-6ffb:
17beta-hydroxysteroid dehydrogenase 14 variant S205 - mutant Q148A - in complex with a nonsteroidal inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6hno:
17beta-hydroxysteroid dehydrogenase 14 variant S205 - mutant H93A
Method: X-RAY DIFFRACTION / Resolution: 1.68 Å

PDB-6qck:
17beta-hydroxysteroid dehydrogenase 14 variant T205 in complex with FB262
Method: X-RAY DIFFRACTION / Resolution: 1.68 Å

Chemicals

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

ChemComp-NA:
Unknown entry

ChemComp-BGC:
beta-D-glucopyranose

ChemComp-F45:
[6-(3,4-dihydroxyphenyl)pyridin-2-yl](4-fluoro-3-hydroxyphenyl)methanone

ChemComp-HOH:
WATER

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HWK:
2-[2-(1,3-benzodioxol-2-yl)ethyl]benzoic acid

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / 17b-HSD14 / mutation / inhibition / fragments / soaking

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