1D1W

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)

1D1W の概要

• エントリーDOI: 10.2210/pdb1d1w/pdb
• 関連するPDBエントリー: 1D0C 1D0O 1D1V 1D1W 1D1X 1D1Y 1NSE
• 分子名称: NITRIC OXIDE SYNTHASE, ACETATE ION, ZINC ION, ... (9 entities in total)
• 機能のキーワード: alpha-beta fold, oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cell membrane: P29473
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102285.95

構造登録者

Li, H.,Raman, C.S.,Martasek, P.,Kral, V.,Masters, B.S.S.,Poulos, T.L. (登録日: 1999-09-21, 公開日: 2000-10-25, 最終更新日: 2024-02-07)

主引用文献

Li, H.,Raman, C.S.,Martasek, P.,Kral, V.,Masters, B.S.,Poulos, T.L.
Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.
J.Inorg.Biochem., 81:133-139, 2000

PubMed Abstract: Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.

PubMed: 11051558
DOI: 10.1016/S0162-0134(00)00099-4

実験手法

X-RAY DIFFRACTION (2 Å)