1fax
From Proteopedia
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| , resolution 3.0Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Coagulation factor Xa, with EC number 3.4.21.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COAGULATION FACTOR XA INHIBITOR COMPLEX
Contents |
Overview
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 natural substrate recognition as well as for drug design.
Disease
Known disease associated with this structure: Factor X deficiency OMIM:[227600]
About this Structure
1FAX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
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:8939944
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