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Structure paper

TitleCofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation.
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 16778-16785, Year 2004
Publish dateSep 12, 2003 (structure data deposition date)
AuthorsShi, R. / Lin, S.X.
External linksJ. Biol. Chem. / PubMed:14966133
MethodsX-ray diffraction
Resolution1.63 - 1.89 Å
Structure data

PDB-1qyv:
Crystal structure of human estrogenic 17beta-hydroxysteroid dehydrogenase complex with NADP
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-1qyw:
Crystal structure of human estrogenic 17beta-hydroxysteroid dehydrogenase complex with androstanedione and NADP
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

PDB-1qyx:
Crystal structure of human estrogenic 17beta-hydroxysteroid dehydrogenase complex with androstenedione and NADP
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

Chemicals

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-5SD:
5ALPHA-ANDROSTAN-3,17-DIONE

ChemComp-ASD:
4-ANDROSTENE-3-17-DIONE / hormone*YM

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / 17bHSD1-cofactor complex / 17bHSD1 / androstanedione / C19-steroid / NADP / androstenedione / NADP binding

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