5A6O

Crystal structure of the apo form of the unphosphorylated human death associated protein kinase 3 (DAPK3)

5A6O の概要

• エントリーDOI: 10.2210/pdb5a6o/pdb
• 関連するPDBエントリー: 5A6N
• 分子名称: DEATH-ASSOCIATED PROTEIN KINASE 3, GLYCEROL, S-1,2-PROPANEDIOL, ... (4 entities in total)
• 機能のキーワード: transferase, dapk3, apo, death-associated protein kinase 3, zipper-interacting protein kinase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus . Isoform 1: Nucleus . Isoform 2: Nucleus : O43293
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65518.72

構造登録者

Rodrigues, T.,Reker, D.,Welin, M.,Caldera, M.,Brunner, C.,Gabernet, G.,Schneider, P.,Walse, B.,Schneider, G. (登録日: 2015-06-30, 公開日: 2015-10-21, 最終更新日: 2024-01-10)

主引用文献

Rodrigues, T.,Reker, D.,Welin, M.,Caldera, M.,Brunner, C.,Gabernet, G.,Schneider, P.,Walse, B.,Schneider, G.
De Novo Fragment Design for Drug Discovery and Chemical Biology.
Angew.Chem.Int.Ed.Engl., 54:15079-, 2015

PubMed Abstract: Automated molecular de novo design led to the discovery of an innovative inhibitor of death-associated protein kinase 3 (DAPK3). An unprecedented crystal structure of the inactive DAPK3 homodimer shows the fragment-like hit bound to the ATP pocket. Target prediction software based on machine learning models correctly identified additional macromolecular targets of the computationally designed compound and the structurally related marketed drug azosemide. The study validates computational de novo design as a prime method for generating chemical probes and starting points for drug discovery.

PubMed: 26486226
DOI: 10.1002/ANIE.201508055

実験手法

X-RAY DIFFRACTION (1.6 Å)