3SOR
Factor XIa in complex with a clorophenyl-tetrazole inhibitor
Summary for 3SOR
| Entry DOI | 10.2210/pdb3sor/pdb |
| Descriptor | Coagulation factor XI, CITRIC ACID, {4-[(N-{3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl}-L-phenylalanyl)amino]phenyl}acetic acid, ... (4 entities in total) |
| Functional Keywords | hydrolase, serine protease, coagulation factor, syntethic inhibitor, blood, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P03951 |
| Total number of polymer chains | 1 |
| Total formula weight | 27581.60 |
| Authors | Kazemier, B.,Oubrie, A. (deposition date: 2011-06-30, release date: 2012-04-11, Last modification date: 2024-10-16) |
| Primary citation | Fradera, X.,Kazemier, B.,Carswell, E.,Cooke, A.,Oubrie, A.,Hamilton, W.,Dempster, M.,Krapp, S.,Nagel, S.,Jestel, A. High-resolution crystal structures of factor XIa coagulation factor in complex with nonbasic high-affinity synthetic inhibitors. Acta Crystallogr.,Sect.F, 68:404-408, 2012 Cited by PubMed Abstract: Factor XI (FXI) is a key enzyme in the coagulation pathway and an attractive target for the development of anticoagulant drugs. A small number of high-resolution crystal structures of FXIa in complex with small synthetic inhibitors have been published to date. All of these ligands have a basic P1 group and bind exclusively in the nonprime side of the active site of FXIa. Here, two structures of FXIa in complex with nonbasic inhibitors that occupy both the prime and nonprime sides of the active site are presented. These new structures could be valuable in the design and optimization of new FXIa synthethic inhibitors. PubMed: 22505407DOI: 10.1107/S1744309112009037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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