View source for 2huq


==Crystal structure of PH0725 from Pyrococcus horikoshii OT3==
<StructureSection load='2huq' size='340' side='right'caption='[[2huq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2huq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HUQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hut|2hut]], [[2huv|2huv]], [[2hux|2hux]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Diphthine_synthase Diphthine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.98 2.1.1.98] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2huq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2huq OCA], [https://pdbe.org/2huq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2huq RCSB], [https://www.ebi.ac.uk/pdbsum/2huq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2huq ProSAT], [https://www.topsan.org/Proteins/RSGI/2huq TOPSAN]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/DPHB_PYRHO DPHB_PYRHO]] S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.<ref>PMID:20873788</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/2huq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=2huq ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Diphthine synthase]]
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Karthe, P]]
[[Category: Kumarevel, T S]]
[[Category: Kunishima, N]]
[[Category: Structural genomic]]
[[Category: Sugahara, M]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Pyrococcus horikoshii ot3]]
[[Category: Rsgi]]
[[Category: Transferase]]