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: 15123423 DOI: 10.1016/j.jmb.2004.03.035 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.08 Å)

Structure validation