2C4W

Type II Dehydroquinase from H. pylori in complex with AH9095

2C4W の概要

• エントリーDOI: 10.2210/pdb2c4w/pdb
• 関連するPDBエントリー: 1J2Y 2C4V 2C57
• 分子名称: 3-DEHYDROQUINATE DEHYDRATASE, N-TETRAZOL-5-YL 9-OXO-9H-XANTHENE-2 SULPHONAMIDE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: 3-dehydroquinase, shikimate pathway, aromatic amino acid biosynthesis, lyase, dehydroquinate, sulphonamide
• 由来する生物種: HELICOBACTER PYLORI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20055.95

構造登録者

Robinson, D.A.,Lapthorn, A.J. (登録日: 2005-10-24, 公開日: 2006-02-22, 最終更新日: 2023-12-13)

主引用文献

Robinson, D.A.,Stewart, K.A.,Price, N.C.,Chalk, P.A.,Coggins, J.R.,Lapthorn, A.J.
Crystal Structures of Helicobacter Pylori Type II Dehydroquinase Inhibitor Complexes: New Directions for Inhibitor Design.
J.Med.Chem., 49:1282-, 2006

PubMed Abstract: The crystal structures of the type II dehydroquinase (DHQase) from Helicobacter pylori in complex with three competitive inhibitors have been determined. The inhibitors are the substrate analogue 2,3-anhydroquinate (FA1), citrate, and an oxoxanthene sulfonamide derivative (AH9095). Despite the very different chemical nature of the inhibitors, in each case the primary point of interaction with the enzyme is via the residues that bind the C1 functionalities of the substrate, 3-dehydroquinate, i.e., N76, H102, I103, and H104. The DHQase/AH9095 complex crystal structure shows that sulfonamides can form a scaffold for nonsubstrate-like inhibitors and identifies a large conserved hydrophobic patch at the entrance to the active site as a locus that can be exploited in the development of new ligands.

PubMed: 16480265
DOI: 10.1021/JM0505361

実験手法

X-RAY DIFFRACTION (1.55 Å)