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1UVT

BOVINE THROMBIN--BM14.1248 COMPLEX

Summary for 1UVT
Entry DOI10.2210/pdb1uvt/pdb
DescriptorTHROMBIN, N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE, ... (4 entities in total)
Functional Keywordsserine protease, hydrolase, thrombin, blood coagulation
Biological sourceBos taurus (cattle)
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Cellular locationSecreted, extracellular space: P00735 P00735
Total number of polymer chains2
Total formula weight35892.13
Authors
Engh, R.A.,Huber, R. (deposition date: 1996-10-16, release date: 1997-11-19, Last modification date: 2024-10-30)
Primary citationEngh, 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: 8939759
DOI: 10.1016/S0969-2126(96)00142-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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