5FYD
Structural and biochemical insights into 7beta-hydroxysteroid dehydrogenase stereoselectivity
5FYD の概要
| エントリーDOI | 10.2210/pdb5fyd/pdb |
| 分子名称 | OXIDOREDUCTASE, SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY PROTEIN, GLYCEROL (3 entities in total) |
| 機能のキーワード | oxidoreductase, short-chain dehydrogenase, steroid, stereoselectivity, dehydrogenase |
| 由来する生物種 | COLLINSELLA AEROFACIENS |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 57659.65 |
| 構造登録者 | Savino, S.,Ferrandi, E.,Forneris, F.,Rovida, S.,Riva, S.,Monti, D.,Mattevi, A. (登録日: 2016-03-07, 公開日: 2016-04-06, 最終更新日: 2024-01-10) |
| 主引用文献 | Savino, S.,Ferrandi, E.E.,Forneris, F.,Rovida, S.,Riva, S.,Monti, D.,Mattevi, A. Structural and Biochemical Insights Into 7Beta-Hydroxysteroid Dehydrogenase Stereoselectivity. Proteins, 84:859-, 2016 Cited by PubMed Abstract: Hydroxysteroid dehydrogenases are of great interest as biocatalysts for transformations involving steroid substrates. They feature a high degree of stereo- and regio-selectivity, acting on a defined atom with a specific configuration of the steroid nucleus. The crystal structure of 7β-hydroxysteroid dehydrogenase from Collinsella aerofaciens reveals a loop gating active-site accessibility, the bases of the specificity for NADP(+) , and the general architecture of the steroid binding site. Comparison with 7α-hydroxysteroid dehydrogenase provides a rationale for the opposite stereoselectivity. The presence of a C-terminal extension reshapes the substrate site of the β-selective enzyme, possibly leading to an inverted orientation of the bound substrate. Proteins 2016; 84:859-865. © 2016 Wiley Periodicals, Inc. PubMed: 27006087DOI: 10.1002/PROT.25036 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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