1fax
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COAGULATION FACTOR XA INHIBITOR COMPLEX
OverviewOverview
The 3.0-A resolution x-ray structure of human des-Gla-coagulation factor, Xa (fXa) has been determined in complex with the synthetic inhibitor, DX-9065a. The binding geometry is characterized primarily by two, interaction sites: the naphthamidine group is fixed in the S1 pocket by a, typical salt bridge to Asp-189, while the pyrrolidine ring binds in the, unique aryl-binding site (S4) of fXa. Unlike the large majority of, inhibitor complexes with serine proteinases, Gly-216 (S3) does not, contribute to hydrogen bond formation. In contrast to typical thrombin, binding modes, the S2 site of fXa cannot be used by DX-9065a since it is, blocked by Tyr-99, and the aryl-binding site (S4) of fXa is lined by, carbonyl oxygen atoms that can accommodate positive charges. This has, implications for ... [(full description)]
About this StructureAbout this Structure
1FAX is a [Protein complex] structure of sequences from [Homo sapiens] with CA and DX9 as [ligands]. Active as [Coagulation factor Xa], with EC number [3.4.21.6]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition., Brandstetter H, Kuhne A, Bode W, Huber R, von der Saal W, Wirthensohn K, Engh RA, J Biol Chem. 1996 Nov 22;271(47):29988-92. PMID:8939944
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