1xok
From Proteopedia
(Difference between revisions)
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<StructureSection load='1xok' size='340' side='right'caption='[[1xok]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1xok' size='340' side='right'caption='[[1xok]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1xok]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOK OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[1xok]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XOK FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xok OCA], [https://pdbe.org/1xok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xok RCSB], [https://www.ebi.ac.uk/pdbsum/1xok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xok ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/CAPSD_AMVYS CAPSD_AMVYS]] Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity). |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 16:40, 27 October 2021
crystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptide
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