2p5c
From Proteopedia
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| - | [[Image:2p5c.jpg|left|200px]] | ||
| - | + | ==Crystal structure of PH0725 from Pyrococcus horikoshii OT3== | |
| - | + | <StructureSection load='2p5c' size='340' side='right'caption='[[2p5c]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[2p5c]] 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=2P5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P5C 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]] 2.4Å</td></tr> | |
| - | + | <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=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=2p5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p5c OCA], [https://pdbe.org/2p5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p5c RCSB], [https://www.ebi.ac.uk/pdbsum/2p5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p5c ProSAT], [https://www.topsan.org/Proteins/RSGI/2p5c 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/p5/2p5c_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=2p5c ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Diphthine synthase|Diphthine synthase]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Pyrococcus horikoshii | + | [[Category: Large Structures]] |
| - | + | [[Category: Pyrococcus horikoshii OT3]] | |
| - | [[Category: Kunishima | + | [[Category: Kunishima N]] |
| - | [[Category: Matsuura | + | [[Category: Matsuura Y]] |
| - | [[Category: Ono | + | [[Category: Ono N]] |
| - | + | [[Category: Taketa M]] | |
| - | [[Category: Taketa | + | [[Category: Yamamoto H]] |
| - | [[Category: Yamamoto | + | |
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Current revision
Crystal structure of PH0725 from Pyrococcus horikoshii OT3
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