2pca: Difference between revisions
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New page: left|200px<br /><applet load="2pca" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pca, resolution 2.00Å" /> '''Crystal structure of... |
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== | ==Crystal structure of PH0725 from Pyrococcus horikoshii OT3== | ||
<StructureSection load='2pca' size='340' side='right'caption='[[2pca]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
[[Category: | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pca]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PCA 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]] 2Å</td></tr> | |||
<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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pca OCA], [https://pdbe.org/2pca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pca RCSB], [https://www.ebi.ac.uk/pdbsum/2pca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pca ProSAT], [https://www.topsan.org/Proteins/RSGI/2pca 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/pc/2pca_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=2pca ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Diphthine synthase|Diphthine synthase]] | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Kunishima N]] | |||
[[Category: Kunishima | [[Category: Matsuura Y]] | ||
[[Category: Matsuura | [[Category: Morikawa Y]] | ||
[[Category: Morikawa | [[Category: Sugahara M]] | ||
[[Category: Taketa M]] | |||
[[Category: Sugahara | |||
[[Category: Taketa | |||
Latest revision as of 09:00, 25 October 2023
Crystal structure of PH0725 from Pyrococcus horikoshii OT3
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