2e3x
From Proteopedia
(Difference between revisions)
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<StructureSection load='2e3x' size='340' side='right' caption='[[2e3x]], [[Resolution|resolution]] 2.91Å' scene=''> | <StructureSection load='2e3x' size='340' side='right' caption='[[2e3x]], [[Resolution|resolution]] 2.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Dabsi Dabsi]. 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 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> | </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 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 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 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> | + | <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://pdbe.org/2e3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e3x RCSB], [http://www.ebi.ac.uk/pdbsum/2e3x PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/VM3CX_DABSI VM3CX_DABSI]] 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/SLLC1_DABSI SLLC1_DABSI]] 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/SLLC2_DABSI SLLC2_DABSI]] 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Dabsi]] |
[[Category: Russellysin]] | [[Category: Russellysin]] | ||
[[Category: Igarashi, T]] | [[Category: Igarashi, T]] | ||
Revision as of 09:08, 10 September 2015
Crystal structure of Russell's viper venom metalloproteinase
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Categories: Dabsi | Russellysin | Igarashi, T | Takeda, S | Blood clotting | C-type lectin | Disintegrin | Hydrolase | Metalloproteinase | Toxin
