2HSD
THE REFINED THREE-DIMENSIONAL STRUCTURE OF 3ALPHA,20BETA-HYDROXYSTEROID DEHYDROGENASE AND POSSIBLE ROLES OF THE RESIDUES CONSERVED IN SHORT-CHAIN DEHYDROGENASES
「1HSD」から置き換えられました2HSD の概要
| エントリーDOI | 10.2210/pdb2hsd/pdb |
| 分子名称 | 3-ALPHA, 20 BETA-HYDROXYSTEROID DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (2 entities in total) |
| 機能のキーワード | oxidoreductase |
| 由来する生物種 | Streptomyces exfoliatus |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 107760.08 |
| 構造登録者 | |
| 主引用文献 | Ghosh, D.,Wawrzak, Z.,Weeks, C.M.,Duax, W.L.,Erman, M. The refined three-dimensional structure of 3 alpha,20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure, 2:629-640, 1994 Cited by PubMed Abstract: Bacterial 3 alpha,20 beta-hydroxysteroid dehydrogenase reversibly oxidizes the 3 alpha and 20 beta hydroxyl groups of steroids derived from androstanes and pregnanes. It was the first short-chain dehydrogenase to be studied by X-ray crystallography. The previous description of the structure of this enzyme, at 2.6 A resolution, did not permit unambiguous assignment of several important groups. We have further refined the structure of the complex of the enzyme with its cofactor, nicotinamide adenine dinucleotide (NAD), and solvent molecules, at the same resolution. PubMed: 7922040DOI: 10.1016/S0969-2126(00)00064-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.64 Å) |
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