2XLN

Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor

2XLN の概要

• エントリーDOI: 10.2210/pdb2xln/pdb
• 関連するPDBエントリー: 1W79 1W8Q 1W8Y 2VGJ 2VGK 2WKE 2XDM 2XK1 2Y4A 2Y55 2Y59
• 分子名称: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,, [(1S)-1-{[(2,6-DIMETHOXYPHENYL)CARBONYL]AMINO}ETHYL]BORONIC ACID, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, peptidoglycan
• 由来する生物種: ACTINOMADURA SP
• 細胞内の位置: Secreted: P39045
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 203098.42

構造登録者

Sauvage, E.,Herman, R.,Kerff, F.,Rocaboy, M.,Charlier, P. (登録日: 2010-07-21, 公開日: 2011-01-26, 最終更新日: 2014-06-18)

主引用文献

Woon, E.C.Y.,Zervosen, A.,Sauvage, E.,Simmons, K.J.,Ivec, M.,Inglis, S.R.,Fishwick, C.W.G.,Gobec, S.,Charlier, P.,Luxen, A.,Schofield, C.J.
Structure Guided Development of Potent Reversibly Binding Penicillin Binding Protein Inhibitors
Acs Med.Chem.Lett., 2:219-, 2011

PubMed Abstract: Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as β-lactams.

PubMed: 24900305
DOI: 10.1021/ML100260X

実験手法

X-RAY DIFFRACTION (2.4 Å)