1UVT
BOVINE THROMBIN--BM14.1248 COMPLEX
Summary for 1UVT
Entry DOI | 10.2210/pdb1uvt/pdb |
Descriptor | THROMBIN, N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE, ... (4 entities in total) |
Functional Keywords | serine protease, hydrolase, thrombin, blood coagulation |
Biological source | Bos taurus (cattle) More |
Cellular location | Secreted, extracellular space: P00735 P00735 |
Total number of polymer chains | 2 |
Total formula weight | 35892.13 |
Authors | Engh, R.A.,Huber, R. (deposition date: 1996-10-16, release date: 1997-11-19, Last modification date: 2024-10-30) |
Primary citation | Engh, R.A.,Brandstetter, H.,Sucher, G.,Eichinger, A.,Baumann, U.,Bode, W.,Huber, R.,Poll, T.,Rudolph, R.,von der Saal, W. Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: implications for drug design. Structure, 4:1353-1362, 1996 Cited by PubMed Abstract: The explosive growth in the rate of X-ray determination of protein structures is fuelled largely by the expectation that structural information will be useful for pharmacological and biotechnological applications. For example, there have been intensive efforts to develop orally administrable antithrombotic drugs using information about the crystal structures of blood coagulation factors, including thrombin. Most of the low molecular weight thrombin inhibitors studied so far are based on arginine and benzamidine. We sought to expand the database of information on thrombin-inhibitor binding by studying new classes of inhibitors. PubMed: 8939759DOI: 10.1016/S0969-2126(96)00142-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report