1BCU

ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN

1BCU の概要

• エントリーDOI: 10.2210/pdb1bcu/pdb
• 分子名称: ALPHA-THROMBIN, HIRUGEN, PROFLAVIN, ... (5 entities in total)
• 機能のキーワード: complex (serine protease inhibitor), hydrolase, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Hirudo medicinalis (medicinal leech); 詳細
• 細胞内の位置: Secreted, extracellular space: P00734 P00734; Secreted: P01050
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 35634.58

構造登録者

Conti, E.,Rivetti, C.,Wonacott, A.,Brick, P. (登録日: 1998-05-02, 公開日: 1998-10-14, 最終更新日: 2024-10-23)

主引用文献

Conti, E.,Rivetti, C.,Wonacott, A.,Brick, P.
X-ray and spectrophotometric studies of the binding of proflavin to the S1 specificity pocket of human alpha-thrombin.
FEBS Lett., 425:229-233, 1998

PubMed Abstract: Proflavin can be used to study the interactions of inhibitors and substrates with thrombin by monitoring the changes in the visible absorption spectrum that occur on dye displacement. We have used microspectrophotometric methods to investigate the binding of proflavin to crystals of an alpha-thrombin-hirugen complex and have determined the structure by X-ray crystallography. The proflavin molecule binds in the S1 pocket of the enzyme with one of the amino groups hydrogen bonded to the carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen bonded to the carbonyl of Gly-219. This result indicates that the proflavin displacement assay can be used to specifically monitor the binding of inhibitors to the S1 pocket.

PubMed: 9559654
DOI: 10.1016/S0014-5793(98)00235-X

実験手法

X-RAY DIFFRACTION (2 Å)