17beta-estradiol 17-dehydrogenase

This is an abbreviated version, for detailed information about 17beta-estradiol 17-dehydrogenase, go to the full flat file.




(17beta-HSD) type 1, (17beta-HSD) type 2, 17-beta-HSD 2, 17-beta-hydroxysteroid dehydrogenase type 12, 17-beta-hydroxysteroid dehydrogenase type 2, 17-HOR, 17-HSD, 17beta HSD1, 17beta,20alpha-hydroxysteroid dehydrogenase, 17beta-estradiol dehydrogenase, 17beta-HSD, 17beta-hsd 14, 17beta-HSD I, 17beta-HSD type 1, 17beta-HSD type 12, 17beta-HSD type 2, 17beta-HSD type 4, 17beta-HSD type 5, 17beta-HSD type 7, 17beta-HSD type 8, 17beta-HSD1, 17beta-HSD12, 17beta-HSD14, 17beta-HSD2, 17beta-HSD4, 17beta-HSD5, 17beta-HSD7 2, 17beta-HSDcl, 17beta-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase 1, 17beta-hydroxysteroid dehydrogenase 2, 17beta-hydroxysteroid dehydrogenase 4, 17beta-hydroxysteroid dehydrogenase type 1, 17beta-hydroxysteroid dehydrogenase type 12, 17beta-hydroxysteroid dehydrogenase type 14, 17beta-hydroxysteroid dehydrogenase type 2, 17beta-hydroxysteroid dehydrogenase type 4, 17beta-hydroxysteroid dehydrogenase type 5, 17beta-hydroxysteroid dehydrogenase type 6, 17beta-hydroxysteroid dehydrogenase type 7, 17beta-hydroxysteroid dehydrogenase type 8, 17beta-hydroxysteroid dehydrogenase type I, 17beta-hydroxysteroid dehydrogenase type IV, 17beta-hydroxysteroid dehydrogenase types 1, 17beta-hydroxysteroid dehydrogenases type 1, 17betaHSD, 17betaHSD1, 17betaHSD14, 17betaHSD6, 17HSD1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, 20alpha-hydroxysteroid dehydrogenase, 3beta-HSD, 3beta-hydroxysteroid dehydrogenase, 3betaHSD, 7beta-HSD type 1, AKR1B15, AKR1C1, AKR1C2, AKR1C3, AKR1C4, aldo-keto reductase 1B15, dehydrogenase, estradiol 17beta-, E2DH, EDH, estradiol 17beta-dehydrogenase, estradiol dehydrogenase, estrogen 17-oxidoreductase, estrogenic 17beta-hydroxysteroid dehydrogenase, form 2 type 7 17beta-hydroxysteroid dehydrogenase, HSD17B1, HSD17B12, HSD17B2, HSD17B4, hydroxysteroid (17-beta) dehydrogenase 1, Ke6 protein, mf17beta-HSD12, microsomal 17-beta-hydroxysteroid dehydrogenase, More, NlHsd17b12, oestradiol-17beta hydroxysteroid dehydrogenase, placental 17-beta-hydroxysteroid dehydrogenase, PRAP, PRL receptor associated protein, testicular 17-beta-hydroxysteroid dehydrogenase, type 1 17beta-HSD, type 1 17beta-hydroxysteroid dehydrogenase, type 12 17beta-HSD, type 12 17beta-hydroxysteroid dehydrogenase, type 7 17beta-hydroxysteroid dehydrogenase, type 8 17beta-HSD, type 8 17beta-hydroxysteroid dehydrogenase


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


Crystallization on EC - 17beta-estradiol 17-dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
hanging-drop vapour-diffusion method, crystallization of the 17beta-HSDcl apo form and Tyr167Phe mutant, crystals diffract to 1.7 A resolution. The space group is identified as I4(1)22, with unit-call parameters a = b = 67.14, c = 266.77 A
17beta-HSD14 in ternary complex with NADP+ and estradiol, modelling
active site analysis of 17beta-hydroxysteroid dehydrogenase type 1 enzyme complexes (estradiol/NADP+, equilin/NADP+, dehydroepiandrosterone) using the SPROUT program
crystal structure of 17beta-HSD1 complexed with testosterone or estradiol are shown. Both testosterone and estradiol bind in the narrow hydrophobic tunnel of 17beta-HSD1 with a high degree of complementarity. Testosterone is bound in an alternative orientation to 17beta-HSD1 compared with estradiol. Residue L149 plays an important role in the discrimination between C19 androgen and C18 estrogen
crystallization and crystal structure of the complex of the enzyme with the dual-site inhibitor, EM-139
hanging drop vapor diffusion method
in complex with ligands estradiol, equiline, 5-alpha-dihydrotestosterone, O5'-[9-(3,17beta-dihydroxy-1,3,5(10)-estratrien-16beta-yl)nonanoyl]adenosine and 3-[[(16beta,17beta)-3,17-dihydroxyestra-1,3,5(10)trien-16-yl]methyl]benzamide. Construction of pharmacophore model
method for crystallization of a labile enzyme
ternary complex of the 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one and NADP+
the purified enzyme variants T205 and S205 in apoform, as holoenzyme, or in complex with estrone or inhibitor [6-(3,4-dihydroxyphenyl)pyridin-2-yl]-(4-fluoro-3-hydroxyphenyl)methanone, ternary complex enzyme-cofactor-inhibitor, X-ray diffraction structure determination and analysis at 1.52-2.02 A resolution