3DYB

proteinase K- digalacturonic acid complex

3DYB の概要

• エントリーDOI: 10.2210/pdb3dyb/pdb
• 分子名称: Proteinase K, alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: proteinase k, hepes, digalacturonic acid, silverbullets, structural genomics, psi-2, protein structure initiative, center for high-throughput structural biology, chtsb, hydrolase, metal-binding, protease, serine protease, zymogen
• 由来する生物種: Engyodontium album (Engyodontium album)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29647.51

構造登録者

Larson, S.B.,Day, J.S.,McPherson, A.,Cudney, R.,Nguyen, C.,Center for High-Throughput Structural Biology (CHTSB) (登録日: 2008-07-25, 公開日: 2008-10-07, 最終更新日: 2024-11-13)

主引用文献

Larson, S.B.,Day, J.S.,Nguyen, C.,Cudney, R.,McPherson, A.
High-resolution structure of proteinase K cocrystallized with digalacturonic acid.
Acta Crystallogr.,Sect.F, 65:192-198, 2009

PubMed Abstract: Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside the protein, two calcium ions, 379 water molecules, a molecule of DGA and a partially occupied HEPES molecule. The DGA molecule has one sugar moiety disposed exactly on a crystallographic twofold axis; the second ring was not observed. The DGA molecule is bound to two protein molecules across the twofold axis through hydrogen-bonding networks involving Ser150 and water molecules. One of the calcium-ion sites has not been reported previously. This study further illustrates the involvement of small molecules in the crystallization of macromolecules through their ability to form intermolecular lattice interactions.

PubMed: 19255463
DOI: 10.1107/S1744309109002218

実験手法

X-RAY DIFFRACTION (1.32 Å)