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TitleCrystal Structures of Human Delta4-3-Ketosteroid 5beta-Reductase (AKR1D1) Reveal the Presence of an Alternative Binding Site Responsible for Substrate Inhibition (dagger) (,) (double dagger).
Journal, issue, pagesBiochemistry, Vol. 47, Page 13537-13546, Year 2008
Publish dateFeb 20, 2008 (structure data deposition date)
AuthorsFaucher, F. / Cantin, L. / Luu-The, V. / Labrie, F. / Breton, R.
External linksBiochemistry / PubMed:19075558
MethodsX-ray diffraction
Resolution2 - 2.2 Å
Structure data

PDB-3caq:
Crystal structure of 5beta-reductase (AKR1D1) in complex with NADPH
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3cas:
Crystal structure of 5beta-reductase (AKR1D1) in complex with NADP+ and 4-androstenedione
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

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

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-ASD:
4-ANDROSTENE-3-17-DIONE

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / 5b-reductase / 5beta-reductase / 5b-red / AKR1D1 / AKR / aldo-keto reductase / NADP / androstenedione / NADPH / 5b-dhp / substrate inhibition / Bile acid catabolism / Cytoplasm / Disease mutation / Lipid metabolism / Steroid metabolism

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