6Y5T

Crystal structure of savinase at room temperature

6Y5T の概要

• エントリーDOI: 10.2210/pdb6y5t/pdb
• 分子名称: Subtilisin Savinase, CALCIUM ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: subtilisin savinase, protein dynamics, alternative conformations, hydrolase
• 由来する生物種: Bacillus lentus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26781.45

構造登録者

Wu, S.,Moroz, O.,Turkenburg, J.,Nielsen, J.E.,Wilson, K.S.,Teilum, K. (登録日: 2020-02-25, 公開日: 2020-06-17, 最終更新日: 2024-01-24)

主引用文献

Wu, S.,Nguyen, T.T.T.N.,Moroz, O.V.,Turkenburg, J.P.,Nielsen, J.E.,Wilson, K.S.,Rand, K.D.,Teilum, K.
Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis.
Peerj, 8:e9408-e9408, 2020

PubMed Abstract: Several examples have emerged of enzymes where slow conformational changes are of key importance for function and where low populated conformations in the resting enzyme resemble the conformations of intermediate states in the catalytic process. Previous work on the subtilisin protease, Savinase, from by NMR spectroscopy suggested that this enzyme undergoes slow conformational dynamics around the substrate binding site. However, the functional importance of such dynamics is unknown.

PubMed: 32617193
DOI: 10.7717/peerj.9408

実験手法

X-RAY DIFFRACTION (1.1 Å)