3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)

This is an abbreviated version, for detailed information about 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+), go to the full flat file.




17-ketoreductase, 17beta-HSD, 17beta-hydroxysteroid dehydrogenase type 5, 3alpha(17beta)-HSD, 3alpha(17beta)-hydroxysteroid dehydrogenase, AKR1C26, AKR1C27, AKR1C28, AKR1C3, AKR1C34, aldo-keto reductase 1C3, dehydrogenase, 3alpha,17beta-hydroxy steroid, More, NAD+-dependent 3alpha(17beta)-hydroxysteroid dehydrogenase, NAD+-dependent 3beta(17beta)-hydroxysteroid dehydrogenase, NAD+-linked S-tetralol dehydrogenase, PGER6, type 2 3alpha-HSD, type 2 3alpha-hxdroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 2 3alppha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 3 17beta-hydroxysteroid dehydrogenase, type 5 17beta-HSD, type 5 17beta-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase, 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
       3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)


Crystallization on EC - 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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, with an estimated free energy of binding of ?5 kcal/mol
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
NADP+ and 2'-des-methyl-indomethacin is determined at a resolution of 1.8 A by molecular replacement. The cofactor binding cavity of AKR1C3 is not perturbed upon binding of the inhibitor