2ejj

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(New page: 200px<br /><applet load="2ejj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ejj, resolution 2.10&Aring;" /> '''Mutant K129M structu...)
Current revision (08:41, 25 October 2023) (edit) (undo)
 
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[[Image:2ejj.jpg|left|200px]]<br /><applet load="2ejj" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ejj, resolution 2.10&Aring;" />
 
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'''Mutant K129M structure of PH0725 from Pyrococcus horikoshii OT3'''<br />
 
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==About this Structure==
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==Mutant K129M structure of PH0725 from Pyrococcus horikoshii OT3==
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2EJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SAH:'>SAH</scene>, <scene name='pdbligand=MES:'>MES</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Diphthine_synthase Diphthine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.98 2.1.1.98] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EJJ OCA].
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<StructureSection load='2ejj' size='340' side='right'caption='[[2ejj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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[[Category: Diphthine synthase]]
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== Structural highlights ==
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[[Category: Pyrococcus horikoshii]]
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<table><tr><td colspan='2'>[[2ejj]] 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=2EJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EJJ FirstGlance]. <br>
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[[Category: Single protein]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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[[Category: Shimizu, K.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ejj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ejj OCA], [https://pdbe.org/2ejj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ejj RCSB], [https://www.ebi.ac.uk/pdbsum/2ejj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ejj ProSAT], [https://www.topsan.org/Proteins/RSGI/2ejj TOPSAN]</span></td></tr>
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[[Category: GOL]]
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</table>
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[[Category: MES]]
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== Function ==
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[[Category: NA]]
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[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>
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[[Category: SAH]]
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== Evolutionary Conservation ==
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[[Category: national project on protein structural and functional analyses]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: nppsfa]]
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Check<jmol>
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[[Category: riken structural genomics/proteomics initiative]]
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<jmolCheckbox>
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[[Category: rsgi]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/2ejj_consurf.spt"</scriptWhenChecked>
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[[Category: structural genomics]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: transferase]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2ejj ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:33:13 2008''
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==See Also==
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*[[Diphthine synthase|Diphthine synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pyrococcus horikoshii OT3]]
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[[Category: Shimizu K]]

Current revision

Mutant K129M structure of PH0725 from Pyrococcus horikoshii OT3

PDB ID 2ejj

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