2e3x: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E3X FirstGlance]. <br>
<table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E3X FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GM6:3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE'>GM6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><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=GM6:3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE'>GM6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Russellysin Russellysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.58 3.4.24.58] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Russellysin Russellysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.58 3.4.24.58] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e3x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e3x RCSB], [http://www.ebi.ac.uk/pdbsum/2e3x PDBsum]</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=2e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e3x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e3x RCSB], [http://www.ebi.ac.uk/pdbsum/2e3x PDBsum]</span></td></tr>
<table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/RVVX_DABRU RVVX_DABRU]] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.<ref>PMID:18616470</ref>  [[http://www.uniprot.org/uniprot/LC1_DABRU LC1_DABRU]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref>  [[http://www.uniprot.org/uniprot/LC2_DABRU LC2_DABRU]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Daboia russellii siamensis]]
[[Category: Daboia russellii siamensis]]
[[Category: Russellysin]]
[[Category: Russellysin]]
[[Category: Igarashi, T.]]
[[Category: Igarashi, T]]
[[Category: Takeda, S.]]
[[Category: Takeda, S]]
[[Category: Blood clotting]]
[[Category: Blood clotting]]
[[Category: C-type lectin]]
[[Category: C-type lectin]]