5G1A

Bordetella Alcaligenes HDAH bound to PFSAHA

5G1A の概要

• エントリーDOI: 10.2210/pdb5g1a/pdb
• 関連するPDBエントリー: 5G0X 5G0Y 5G10 5G11 5G12 5G13 5G17 5G1B 5G1C
• 分子名称: HISTONE DEACETYLASE-LIKE AMIDOHYDROLASE, ZINC ION, POTASSIUM ION, ... (7 entities in total)
• 機能のキーワード: hydrolase, hdah, hdac, hdlp
• 由来する生物種: ALCALIGENES
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81988.83

構造登録者

Kraemer, A.,Meyer-Almes, F.J.,Yildiz, O. (登録日: 2016-03-24, 公開日: 2017-04-12, 最終更新日: 2024-01-10)

主引用文献

Meyners, C.,Kramer, A.,Yildiz, O.,Meyer-Almes, F.J.
The thermodynamic signature of ligand binding to histone deacetylase-like amidohydrolases is most sensitive to the flexibility in the L2-loop lining the active site pocket.
Biochim. Biophys. Acta, 1861:1855-1863, 2017

PubMed Abstract: The analysis of the thermodynamic driving forces of ligand-protein binding has been suggested to be a key component for the selection and optimization of active compounds into drug candidates. The binding enthalpy as deduced from isothermal titration calorimetry (ITC) is usually interpreted assuming single-step binding of a ligand to one conformation of the target protein. Although successful in many cases, these assumptions are oversimplified approximations of the reality with flexible proteins and complicated binding mechanism in many if not most cases. The relationship between protein flexibility and thermodynamic signature of ligand binding is largely understudied.

PubMed: 28389333
DOI: 10.1016/j.bbagen.2017.04.001

実験手法

X-RAY DIFFRACTION (1.42 Å)