2o5r
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2o5r" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o5r, resolution 2.340Å" /> '''Crystal structure o...) |
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| - | [[Image:2o5r.gif|left|200px]]<br /><applet load="2o5r" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2o5r, resolution 2.340Å" /> | ||
| - | '''Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution== |
| - | + | <StructureSection load='2o5r' size='340' side='right'caption='[[2o5r]], [[Resolution|resolution]] 2.34Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2o5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O5R 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]] 2.34Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2o5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o5r OCA], [https://pdbe.org/2o5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o5r RCSB], [https://www.ebi.ac.uk/pdbsum/2o5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o5r ProSAT], [https://www.topsan.org/Proteins/JCSG/2o5r TOPSAN]</span></td></tr> |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/SYE1_THEMA SYE1_THEMA] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity). | |
| - | [ | + | == 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/o5/2o5r_consurf.spt"</scriptWhenChecked> | |
| - | [ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2o5r ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima]] | ||
Current revision
Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution
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