5FOQ

Acetylcholinesterase in complex with C7653

5FOQ の概要

• エントリーDOI: 10.2210/pdb5foq/pdb
• 関連するPDBエントリー: 5FPP 5FPQ
• 分子名称: ACETYLCHOLINESTERASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-(2,4-dichlorophenoxy)-N-[4-(1-piperidinylmethyl)phenyl]acetamide, ... (6 entities in total)
• 機能のキーワード: hydrolase, signaling protein, quantum chemistry, density functional theory, drug design
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122695.15

構造登録者

Berg, L.,Mishra, B.K.,Andersson, D.C.,Ekstrom, F.,Linusson, A. (登録日: 2015-11-25, 公開日: 2016-03-02, 最終更新日: 2024-10-23)

主引用文献

Berg, L.,Mishra, B.K.,Andersson, C.D.,Ekstrom, F.,Linusson, A.
The Nature of Activated Non-Classical Hydrogen Bonds: A Case Study on Acetylcholinesterase-Ligand Complexes.
Chemistry, 22:2672-, 2016

PubMed Abstract: Molecular recognition events in biological systems are driven by non-covalent interactions between interacting species. Here, we have studied hydrogen bonds of the CH⋅⋅⋅Y type involving electron-deficient CH donors using dispersion-corrected density functional theory (DFT) calculations applied to acetylcholinesterase-ligand complexes. The strengths of CH⋅⋅⋅Y interactions activated by a proximal cation were considerably strong; comparable to or greater than those of classical hydrogen bonds. Significant differences in the energetic components compared to classical hydrogen bonds and non-activated CH⋅⋅⋅Y interactions were observed. Comparison between DFT and molecular mechanics calculations showed that common force fields could not reproduce the interaction energy values of the studied hydrogen bonds. The presented results highlight the importance of considering CH⋅⋅⋅Y interactions when analysing protein-ligand complexes, call for a review of current force fields, and opens up possibilities for the development of improved design tools for drug discovery.

PubMed: 26751405
DOI: 10.1002/CHEM.201503973

実験手法

X-RAY DIFFRACTION (2.3 Å)