1fax: Difference between revisions
New page: left|200px<br /> <applet load="1fax" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fax, resolution 3.0Å" /> '''COAGULATION FACTOR X... |
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==About this Structure== | ==About this Structure== | ||
1FAX is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and DX9 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAX OCA]]. | 1FAX is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and DX9 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAX OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8939944 8939944] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8939944 8939944] | ||
[[Category: Coagulation factor Xa]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
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Revision as of 12:57, 30 October 2007
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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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