2e8q: Difference between revisions

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-[[Image:2e8q.png|left|200px]]
-{{STRUCTURE_2e8q|  PDB=2e8q  |  SCENE=  }}
+==Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M)==
+<StructureSection load='2e8q' size='340' side='right'caption='[[2e8q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-===Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M)===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2e8q]] 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=2E8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8Q 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]] 2.5&#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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-[[2e8q]] 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=2E8Q OCA].
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8q OCA], [https://pdbe.org/2e8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8q RCSB], [https://www.ebi.ac.uk/pdbsum/2e8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8q ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8q TOPSAN]</span></td></tr>
-[[Category: Diphthine synthase]]
+</table>
-[[Category: Pyrococcus horikoshii]]
+== Function ==
-[[Category: Asada, Y.]]
+[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: Kunishima, N.]]
+== Evolutionary Conservation ==
-[[Category: Nakamoto, T.]]
+[[Image:Consurf_key_small.gif|200px|right]]
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+Check<jmol>
-[[Category: Shimada, H.]]
+  <jmolCheckbox>
-[[Category: Taketa, M.]]
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/2e8q_consurf.spt"</scriptWhenChecked>
-[[Category: National project on protein structural and functional analyse]]
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-[[Category: Nppsfa]]
+    <text>to colour the structure by Evolutionary Conservation</text>
-[[Category: Riken structural genomics/proteomics initiative]]
+  </jmolCheckbox>
-[[Category: Rsgi]]
+</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=2e8q ConSurf].
-[[Category: Structural genomic]]
+<div style="clear:both"></div>
-[[Category: Transferase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pyrococcus horikoshii OT3]]
+[[Category: Asada Y]]
+[[Category: Kunishima N]]
+[[Category: Nakamoto T]]
+[[Category: Shimada H]]
+[[Category: Taketa M]]