EC Number |
Reference |
---|
1.1.1.50 | - |
389522, 389548 |
1.1.1.50 | 3alpha-HSD3-NADP+-progesterone complex and 3alpha-HSD3 mutant V54L-NADP+-progesterone complex, sitting drop vapor diffusion method, room temperature, the reservoir solution contains 100 mM sodium cacodylate, pH 6.0, 200 mM ammonium sulfate, 24-26% w/v PEG 3350, with 0.8 mM progesterone, 3-14 days, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, molecular replacement with search model, PDB ID 1J96. Progesterone adopts two different binding modes to form complexes within the wild-type enzyme, with one binding mode similar to the orientation of a bile acid (ursodeoxycholate) in the reported ternary complex of human 3alpha-HSD3-NADP+-ursodeoxycholate and the other binding mode resembling the orientation of 20alpha-OHProg in the ternary complex of human 20alpha-HSD-NADP+-20alpha-OHProg |
738928 |
1.1.1.50 | alpha/beta-barrel, NADP+ is bound in an extended conformation, type III isoform |
389550 |
1.1.1.50 | association to dimer during crystallization |
389523 |
1.1.1.50 | crystal structure of human 3alpha-HSD3-NADP(+)/5alpha-androstane-3,17-dione/epiandrosterone complex obtained by co-crystallization with 5alpha-androstane-3,17-dione (5alpha-DHT) in the presence of NADP+. Although 5alpha-DHT is introduced during the crystallization, oxidoreduction of 5alpha-DHT occurs. The locations of 5alpha-androstane-3,17-dione and epiandrosterone are identified in the steroid-binding sites of two 3alpha-HSD3 molecules per crystal asymmetric unit. An overlay shows that 5alpha-androstane-3,17-dione and epiandrosterone are oriented upside-down and flipped relative to each other, providing structural clues for 5alpha-DHT reverse binding in the enzyme with the generation of different products |
740017 |
1.1.1.50 | isozyme AKR1C2 in ternary complex with NADP+ and ursodeoxycholate, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement |
655214 |
1.1.1.50 | isozyme AKR1C9 in ternary complex with NADP+ and ursodeoxycholate, X-ray diffraction structure determination and analysis at 2.8 A resolution |
655214 |
1.1.1.50 | purified enzyme with NADH, hanging drop vapour diffusion method, 4°C, in presence of 1.4 M ammonium sulfate, 0.14 M NaCl, and 0.1 M Tris, pH 9.0, rod cluster crystals appear within 1 week, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling |
674674 |
1.1.1.50 | purified recombinant enzyme in complex with NADH, hanging drop vapour diffusion method and microseeding, 0.002 ml of protein solution with 0.3 mM 3alpha-HSD and 0.4 mM NADH in 10 mM TrisHCl pH 8.0, are mixed with 0.002 ml reservoir solution optimally containing 0.1 M TrisHCl, pH 9.0, 0.14 M sodium chloride and 1.4 M ammonium sulfate, 4°C, X-ray diffraction structure determination and analysis at 1.8 A resolution |
671112 |
1.1.1.50 | recombinant type 3 isozyme AKR1C2 in complex with NADP+ and ursodeoxycholate, X-ray structure determination and analysis at 3.0 A resolution |
656651 |