1Q13
Crystal structure of rabbit 20alpha hyroxysteroid dehydrogenase in ternary complex with NADP and testosterone
Summary for 1Q13
Entry DOI | 10.2210/pdb1q13/pdb |
Descriptor | Prostaglandin-E2 9-reductase, SULFATE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
Functional Keywords | 20alpha-hsd, hydroxysteroid dehydrogenase, aldo-keto reductase, tim-barrel, akr, testosterone, ternary complex, oxidoreductase |
Biological source | Oryctolagus cuniculus (rabbit) |
Cellular location | Cytoplasm: P80508 |
Total number of polymer chains | 2 |
Total formula weight | 75311.76 |
Authors | Couture, J.-F.,Cantin, L.,Legrand, P.,Luu-The, V.,Labrie, F.,Breton, R. (deposition date: 2003-07-18, release date: 2004-11-16, Last modification date: 2024-02-14) |
Primary citation | Couture, J.F.,Legrand, P.,Cantin, L.,Labrie, F.,Luu-The, V.,Breton, R. Loop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily. J. Mol. Biol., 339:89-102, 2004 Cited by PubMed: 15123423DOI: 10.1016/j.jmb.2004.03.035 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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