1G2L
FACTOR XA INHIBITOR COMPLEX
Summary for 1G2L
Entry DOI | 10.2210/pdb1g2l/pdb |
Descriptor | COAGULATION FACTOR X, CALCIUM ION, [(1-{2[(4-CARBAMIMIDOYL-PHENYLAMINO)-METHYL]-1-METHYL-1H-BENZOIMIDAZOL-5-YL}-CYCLOPROPYL)-PYRIDIN-2-YL-METHYLENEAMINOOXY]-ACETIC ACID ETHYL ESTER, ... (5 entities in total) |
Functional Keywords | blood coagulation, factor xa, inhibitor complexes, serine proteinase, blood coagulation cascade, hydrolase |
Biological source | Homo sapiens (human) More |
Cellular location | Secreted: P00742 P00742 |
Total number of polymer chains | 2 |
Total formula weight | 37411.33 |
Authors | |
Primary citation | Nar, H.,Bauer, M.,Schmid, A.,Stassen, J.M.,Wienen, W.,Priepke, H.W.,Kauffmann, I.K.,Ries, U.J.,Hauel, N.H. Structural basis for inhibition promiscuity of dual specific thrombin and factor Xa blood coagulation inhibitors. Structure, 9:29-38, 2001 Cited by PubMed Abstract: A major current focus of pharmaceutical research is the development of selective inhibitors of the blood coagulation enzymes thrombin or factor Xa to be used as orally bioavailable anticoagulant drugs in thromboembolic disorders and in the prevention of venous and arterial thrombosis. Simultaneous direct inhibition of thrombin and factor Xa by synthetic proteinase inhibitors as a novel approach to antithrombotic therapy could result in potent anticoagulants with improved pharmacological properties. PubMed: 11342132DOI: 10.1016/S0969-2126(00)00551-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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