2dek: Difference between revisions

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-[[Image:2dek.png|left|200px]]
-{{STRUCTURE_2dek|  PDB=2dek  |  SCENE=  }}
+==Crystal structure of project ID PH0725 from Pyrococcus horikoshii OT3 at 1.65 A resolution==
+<StructureSection load='2dek' size='340' side='right'caption='[[2dek]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-===Crystal structure of project ID PH0725 from Pyrococcus horikoshii OT3 at 1.65 A resolution===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2dek]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DEK FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
-==About this Structure==
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-[[2dek]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DEK OCA].
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dek OCA], [https://pdbe.org/2dek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dek RCSB], [https://www.ebi.ac.uk/pdbsum/2dek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dek ProSAT], [https://www.topsan.org/Proteins/RSGI/2dek TOPSAN]</span></td></tr>
-[[Category: Diphthine synthase]]
+</table>
-[[Category: Pyrococcus horikoshii]]
+== Function ==
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+[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>
-[[Category: Shimizu, K.]]
+== Evolutionary Conservation ==
-[[Category: Alpha/beta fold]]
+[[Image:Consurf_key_small.gif|200px|right]]
-[[Category: Antiparallel beta-sheet]]
+Check<jmol>
-[[Category: National project on protein structural and functional analyse]]
+  <jmolCheckbox>
-[[Category: Nppsfa]]
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/2dek_consurf.spt"</scriptWhenChecked>
-[[Category: Riken structural genomics/proteomics initiative]]
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-[[Category: Rsgi]]
+    <text>to colour the structure by Evolutionary Conservation</text>
-[[Category: Structural genomic]]
+  </jmolCheckbox>
-[[Category: Transferase]]
+</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=2dek ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pyrococcus horikoshii OT3]]
+[[Category: Shimizu K]]