1BCU

ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN

Summary for 1BCU

• Entry DOI: 10.2210/pdb1bcu/pdb
• Descriptor: ALPHA-THROMBIN, HIRUGEN, PROFLAVIN, ... (5 entities in total)
• Functional Keywords: complex (serine protease inhibitor), hydrolase, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Hirudo medicinalis (medicinal leech); More
• Cellular location: Secreted, extracellular space: P00734 P00734; Secreted: P01050
• Total number of polymer chains: 3
• Total formula weight: 35634.58

Authors

Conti, E.,Rivetti, C.,Wonacott, A.,Brick, P. (deposition date: 1998-05-02, release date: 1998-10-14, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)