testosterone 17beta-dehydrogenase (NADP+)

This is an abbreviated version, for detailed information about testosterone 17beta-dehydrogenase (NADP+), go to the full flat file.




17-ketoreductase, 17beta-HSD, 17beta-HSD 3, 17beta-HSD type 3, 17beta-HSD type 5, 17beta-HSD-3, 17beta-HSD1, 17beta-HSD3, 17beta-HSD4, 17beta-HSD5, 17beta-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase 3, 17beta-hydroxysteroid dehydrogenase type 3, 17beta-hydroxysteroid dehydrogenase type 5, 17beta-hydroxysteroid dehydrogenases type 3, 17betaHSD3, 3beta-hydroxysteroid dehydrogenase type 3, AKR1C3, HSD17B3, More, NADP-dependent testosterone-17beta-oxidoreductase, type 3 17beta-HSD, type 3 17beta-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase, type 5 beta-hydroxysteroid dehydrogenase


     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
       testosterone 17beta-dehydrogenase (NADP+)


Crystallization on EC - testosterone 17beta-dehydrogenase (NADP+)

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10 ns molecular dynamics simulations of inhibitor bound to isofrom AKR1C3. Binding could induce conformational changes to both inhibitor and enzyme. The compound presumably assumes a stable, energetically favored, planar conformation
docking of inhibitors (2E)-3-(4-methylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-ethylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-bromophenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid and (2E)-3-[4-(methylsulfanyl)phenyl]-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid to crystal structure. Compounds occupy a similar position of the active site as the co-crystallized indomethacin, with the Aryl1 overlapping with the p-chlorobenzoyl moiety of the indomethacin and the Aryl2 overlapping with an indole part of the indomethacin
in complex with 3-phenoxybenzoic acid, to 1.68 A resolution, space group P212121
in complex with inhibitor 1-(4-[[(2R)-2-methylpiperidin-1-yl]sulfonyl]phenyl)-1,3-dihydro-2H-pyrrol-2-one. The 2-pyrrolidinone does not interact directly with residues in the oxyanion hole
in complex with inhibitor 3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid. Compound adopts a similar binding orientation as flufenamic acid, however, its phenylamino ring projects deeper into a subpocket and confers selectivity over the other AKR1C isoforms
purified recombinant enzyme in ternary complex with NADP+ and one inhibitor, from inhibitors 1-6, 15 mg/ml protein in 10 mM potassium phosphate pH 7.4, 500 mM NaCl, 1 mM ethylenediaminetetraacetic acid, 1 mM dithiothreitol is mixed with crystallization solution containing 0.1 M sodium citrate, pH 5.5, 0.4 M ammonium acetate, 2.5% v/v 2-methyl-2,4-pentanediol, 22-30% w/v PEG 4000 for inhibitors 1-4, and containing 0.1 M HEPES pH 6.5, 0.2 M ammonium dihydrogen phosphate, 20-25% w/v PEG 3350 for inhibitors 5 and 6, X-ray diffraction structure determination analysis at 1.55-2.81 A resolution, modelling