2VWM
Aminopyrrolidine Factor Xa inhibitor
Summary for 2VWM
Entry DOI | 10.2210/pdb2vwm/pdb |
Related | 1C5M 1EZQ 1F0R 1F0S 1FAX 1FJS 1G2L 1G2M 1HCG 1IOE 1IQE 1IQF 1IQG 1IQH 1IQI 1IQJ 1IQK 1IQL 1IQM 1IQN 1KSN 1KYE 1LPG 1LPK 1LPZ 1LQD 1MQ5 1MQ6 1MSX 1NFU 1NFW 1NFX 1NFY 1NL8 1P0S 1V3X 1WU1 1XKA 1XKB 1Z6E 2BMG 2BOH 2BOK 2BQ6 2BQ7 2BQW 2CJI 2FZZ 2G00 2GD4 2J2U 2J34 2J38 2J4I 2J94 2J95 2JKH 2UWL 2UWO 2UWP 2VH0 2VH6 2VVC 2VVU 2VVV 2VWL 2VWN 2VWO 2W26 2W3I 2W3K |
Descriptor | ACTIVATED FACTOR XA HEAVY CHAIN, FACTOR X LIGHT CHAIN, (4R)-4-{[(5-chlorothiophen-2-yl)carbonyl]amino}-N-(cyclopropylmethyl)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)-L-prolinamide, ... (5 entities in total) |
Functional Keywords | hydrolase, cation, plasma, calcium, zymogen, protease, inhibitor, polymorphism, glycoprotein, gamma-carboxyglutamic acid, blood clotting, coagulation factor, hydroxylation, serine protease, egf-like domain, cleavage on pair of basic residues |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Secreted: P00742 P00742 |
Total number of polymer chains | 4 |
Total formula weight | 67657.67 |
Authors | Groebke-Zbinden, K.,Banner, D.W.,Benz, J.M.,Blasco, F.,Decoret, G.,Himber, J.,Kuhn, B.,Panday, N.,Ricklin, F.,Risch, P.,Schlatter, D.,Stahl, M.,Unger, R.,Haap, W. (deposition date: 2008-06-26, release date: 2009-07-07, Last modification date: 2023-12-13) |
Primary citation | Zbinden, K.G.,Anselm, L.,Banner, D.W.,Benz, J.M.,Blasco, F.,Decoret, G.,Himber, J.,Kuhn, B.,Panday, N.,Ricklin, F.,Risch, P.,Schlatter, D.,Stahl, M.,Thomi, S.,Unger, R.,Haap, W. Design of Novel Aminopyrrolidine Factor Xa Inhibitors from a Screening Hit. Eur.J.Med.Chem., 44:2787-, 2009 Cited by PubMed Abstract: Starting from a hit identified by focused screening, 3-aminopyrrolidine factor Xa inhibitors were designed. The binding mode as determined by X-ray structural analysis as well as the pharmacokinetic behaviour of selected compounds is discussed. PubMed: 19200624DOI: 10.1016/J.EJMECH.2008.12.025 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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