2bai: Difference between revisions
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<StructureSection load='2bai' size='340' side='right'caption='[[2bai]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2bai' size='340' side='right'caption='[[2bai]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bai]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2bai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enmgo Enmgo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BAI FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2bai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bai OCA], [https://pdbe.org/2bai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bai RCSB], [https://www.ebi.ac.uk/pdbsum/2bai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bai ProSAT], [https://www.topsan.org/Proteins/CESG/2bai TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/POLG_ENMG3 POLG_ENMG3]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). Protein VP0: VP0 precursor is a component of immature procapsids (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 2bai" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2bai" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> |