1f0t

<StructureSection load='1f0t' size='340' side='right' caption='[[1f0t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1f0t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F0T FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PR1:4-HYDROXY-3-[2-OXO-3-(THIENO[3,2-B]PYRIDINE-2-SULFONYLAMINO)-PYRROLIDIN-1-YLMETHYL]-BENZAMIDINE'>PR1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0t OCA], [http://pdbe.org/1f0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f0t RCSB], [http://www.ebi.ac.uk/pdbsum/1f0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0t ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Involved in the coagulation cascade, factor Xa (FXa) is a serine protease which has received great interest as a potential target for the development of new antithrombotics. Although there is a great wealth of structural data on thrombin complexes, few structures of ligand/FXa complexes have been reported, presumably because of the difficulty in growing crystals. Reproducible crystallization conditions for human des-Gla1-45 coagulation FXa have been found. This has led to an improvement in the diffraction quality of the crystals (about 2.1 A) when compared to the previously reported forms (2.3-2.8 A) thus providing a suitable platform for a structure-based drug design approach. A series of crystal structures of noncovalent inhibitors complexed with FXa have been determined, three of which are presented herein. These include compounds containing the benzamidine moiety and surrogates of the basic group. The benzamidine-containing compound binds in a canonical fashion typical of synthetic serine protease inhibitors. On the contrary, molecules that contain surrogates of the benzamidine group do not make direct hydrogen-bonding interactions with the carboxylate of Asp189 at the bottom of the S1 pocket. The structural data provide a likely explanation for the specificity of these inhibitors and a great aid in the design of bioavailable potent FXa inhibitors.

 

<div class="pdbe-citations 1f0t" style="background-color:#fffaf0;"></div>

== References ==

[[Category: Trypsin]]

[[Category: Becker, M R]]

[[Category: Choi-Sledeski, Y M]]

[[Category: Ewing, W R]]

[[Category: Guilloteau, J P]]

[[Category: Klein, S I]]

[[Category: Maignan, S]]

[[Category: Mikol, V]]

[[Category: Pauls, H W]]

[[Category: Pouzieux, S]]

[[Category: Spada, A P]]

[[Category: Protein-inhibitor complex]]