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1vpx
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1vpx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vpx, resolution 2.40Å" /> '''Crystal structure of...) |
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| - | [[Image:1vpx.gif|left|200px]]<br /><applet load="1vpx" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vpx, resolution 2.40Å" /> | ||
| - | '''Crystal structure of Transaldolase (EC 2.2.1.2) (TM0295) from Thermotoga maritima at 2.40 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of Transaldolase (EC 2.2.1.2) (TM0295) from Thermotoga maritima at 2.40 A resolution== |
| - | + | <StructureSection load='1vpx' size='340' side='right'caption='[[1vpx]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[1vpx]] is a 20 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=1VPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VPX 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=SO4:SULFATE+ION'>SO4</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=1vpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vpx OCA], [https://pdbe.org/1vpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vpx RCSB], [https://www.ebi.ac.uk/pdbsum/1vpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vpx ProSAT], [https://www.topsan.org/Proteins/JCSG/1vpx TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/TAL_THEMA TAL_THEMA] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. |
| - | + | == 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/vp/1vpx_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=1vpx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Transaldolase 3D structures|Transaldolase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima]] | ||
Current revision
Crystal structure of Transaldolase (EC 2.2.1.2) (TM0295) from Thermotoga maritima at 2.40 A resolution
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