1jc6: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_fasciatus Bungarus fasciatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JC6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_fasciatus Bungarus fasciatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JC6 FirstGlance]. <br>
</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=1jc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc6 PDBsum]</span></td></tr>
</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=1jc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc6 OCA], [http://pdbe.org/1jc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/IVB1_BUNFA IVB1_BUNFA]] Dual-function toxin that inhibits both serine proteases (high activity on chymotrypsin (Ki = 18 nM), and low activity on elastase) and voltage-gated potassium channels Kv1.3/KCNA3 (IC(50) = 120.0 nM).<ref>PMID:24243656</ref> <ref>PMID:11562364</ref>   
[[http://www.uniprot.org/uniprot/VKT9_BUNFA VKT9_BUNFA]] Dual-function toxin that inhibits both serine proteases (high activity on chymotrypsin (Ki = 18 nM), and low activity on elastase) and voltage-gated potassium channels Kv1.3/KCNA3 (IC(50) = 120.0 nM).<ref>PMID:11562364</ref> <ref>PMID:24243656</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1jc6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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