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Structure paper

TitleLoop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily.
Journal, issue, pagesJ. Mol. Biol., Vol. 339, Page 89-102, Year 2004
Publish dateJul 18, 2003 (structure data deposition date)
AuthorsCouture, J.F. / Legrand, P. / Cantin, L. / Labrie, F. / Luu-The, V. / Breton, R.
External linksJ. Mol. Biol. / PubMed:15123423
MethodsX-ray diffraction
Resolution1.32 - 2.08 Å
Structure data

PDB-1q13:
Crystal structure of rabbit 20alpha hyroxysteroid dehydrogenase in ternary complex with NADP and testosterone
Method: X-RAY DIFFRACTION / Resolution: 2.08 Å

PDB-1q5m:
Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH
Method: X-RAY DIFFRACTION / Resolution: 1.32 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-TES:
TESTOSTERONE / hormone*YM

ChemComp-HOH:
WATER

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Source
  • oryctolagus cuniculus (rabbit)
KeywordsOXIDOREDUCTASE / 20alpha-HSD / hydroxysteroid dehydrogenase / aldo-keto reductase / TIM-barrel / AKR / testosterone / ternary complex / NADPH / HSD

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