2e8q
From Proteopedia
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| - | [[Image:2e8q.jpg|left|200px]]<br /><applet load="2e8q" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2e8q, resolution 2.50Å" /> | ||
| - | '''Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M)'''<br /> | ||
| - | == | + | ==Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M)== |
| - | + | <StructureSection load='2e8q' size='340' side='right'caption='[[2e8q]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == 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]] 2.5Å</td></tr> | |
| - | [ | + | <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> |
| - | + | <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> | |
| - | [[ | + | </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 == |
| - | [[Category: | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[Category: | + | Check<jmol> |
| - | [[Category: | + | <jmolCheckbox> |
| - | [[Category: | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/2e8q_consurf.spt"</scriptWhenChecked> |
| - | [[Category: | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[Category: | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[Category: | + | </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=2e8q ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
| + | == 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]] | ||
Current revision
Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M)
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