2RG3

Covalent complex structure of elastase

2RG3 の概要

• エントリーDOI: 10.2210/pdb2rg3/pdb
• 関連するPDBエントリー: 1ppg
• 分子名称: Leukocyte elastase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: elastase, complex, covalent, disease mutation, glycoprotein, hydrolase, protease, serine protease, zymogen
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24334.09

構造登録者

Huang, W.,Yamamoto, Y. (登録日: 2007-10-02, 公開日: 2008-07-01, 最終更新日: 2025-03-26)

主引用文献

Huang, W.,Yamamoto, Y.,Li, Y.,Dou, D.,Alliston, K.R.,Hanzlik, R.P.,Williams, T.D.,Groutas, W.C.
X-ray snapshot of the mechanism of inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1-dioxide derivatives.
J.Med.Chem., 51:2003-2008, 2008

PubMed Abstract: The mechanism of action of a general class of mechanism-based inhibitors of serine proteases, including human neutrophil elastase (HNE), has been elucidated by determining the X-ray crystal structure of an enzyme-inhibitor complex. The captured intermediate indicates that processing of inhibitor by the enzyme generates an N-sulfonyl imine functionality that is tethered to Ser195, in accordance with the postulated mechanism of action of this class of inhibitors. The identity of the HNE-N-sulfonyl imine species was further corroborated using electrospray ionization mass spectrometry.

PubMed: 18318470
DOI: 10.1021/jm700966p

実験手法

X-RAY DIFFRACTION (1.8 Å)