EC Number   |
|---|
   1.1.1.62 | - |
| 1.1.1.62 | 17beta-HSD14 in ternary complex with NADP+ and estradiol, modelling |
| 1.1.1.62 | active site analysis of 17beta-hydroxysteroid dehydrogenase type 1 enzyme complexes (estradiol/NADP+, equilin/NADP+, dehydroepiandrosterone) using the SPROUT program |
| 1.1.1.62 | 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 |
| 1.1.1.62 | crystallization and crystal structure of the complex of the enzyme with the dual-site inhibitor, EM-139 |
| 1.1.1.62 | hanging drop vapor diffusion method |
| 1.1.1.62 | hanging-drop vapour diffusion method at 27°C, binary and ternary crystal structures of the enzyme complexed with estrone and NADP+, crystals in this study belonged to the space group P212121 and contain a dimer per asymmetric unit |
| 1.1.1.62 | hanging-drop vapour diffusion method at 27°C, crystallization of the enzyme in complex with estrone and NADP+. His221 is the key residue responsible for the reorganization and stabilization of the reversely bound estrone, leading to the formation of a dead end complex, which exists widely in NADP(H)-preferred enzymes for the regulation of their enzymatic activity |
| 1.1.1.62 | 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 |
| 1.1.1.62 | 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 |
