2C4F

crystal structure of factor VII.stf complexed with pd0297121

Summary for 2C4F

• Entry DOI: 10.2210/pdb2c4f/pdb
• Related: 1AHW 1BF9 1BOY 1CVW 1DAN 1DVA 1F7E 1F7M 1FAK 1FF7 1FFM 1J9C 1JBU 1JPS 1KLI 1KLJ 1NL8 1O5D 1QFK 1TFH 1UJ3 1W0Y 1W2K 1W7X 1W8B 1WQV 1YGC 1Z6J 2BZ6 2HFT
• Descriptor: COAGULATION FACTOR VII PRECURSOR, TISSUE FACTOR PRECURSOR, CALCIUM ION, ... (10 entities in total)
• Functional Keywords: blood coagulation, serine protease, egf, egf-like domain, gla, receptor enzyme, glycoprotein, hydrolase, protease, hydroxylation, lipoprotein, palmitate, transmembrane
• Biological source: HOMO SAPIENS; More
• Total number of polymer chains: 4
• Total formula weight: 67883.25

Authors

Kohrt, J.T.,Zhang, E. (deposition date: 2005-10-18, release date: 2006-10-18, Last modification date: 2025-04-09)

Primary citation

Kohrt, J.T.,Filipski, K.J.,Cody, W.L.,Cai, C.,Dudley, D.A.,Huis, C.A.V.,Willardsen, J.A.,Narasimhan, L.S.,Zhang, E.,Rapundalo, S.T.,Saiya-Cork, K.,Leadley, R.J.,Edmunds, J.J.
The Discovery of Fluoropyridine-Based Inhibitors of the Factor Viia/Tf Complex--Part 2
Bioorg.Med.Chem.Lett., 16:1060-, 2006

PubMed Abstract: The activated factor VII/tissue factor complex (FVIIa/TF) is known to play a key role in the formation of blood clots. Inhibition of this complex may lead to new antithrombotic drugs. A fluoropyridine-based series of FVIIa/TF inhibitors was discovered which utilized a diisopropylamino group for binding in the S2 and S3 binding pockets of the active site of the enzyme complex. In this series, an enhancement in binding affinity was observed by substitution at the 5-position of the hydroxybenzoic acid sidechain. An X-ray crystal structure indicates that amides at this position may increase inhibitor binding affinity through interactions with the S1'/S2' pocket.

PubMed: 16289811
DOI: 10.1016/J.BMCL.2005.10.076

Experimental method

X-RAY DIFFRACTION (1.72 Å)