1vcg
From Proteopedia
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(New page: 200px<br /><applet load="1vcg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vcg, resolution 3.02Å" /> '''Crystal Structure of...) |
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| - | [[Image:1vcg.gif|left|200px]]<br /><applet load="1vcg" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vcg, resolution 3.02Å" /> | ||
| - | '''Crystal Structure of IPP isomerase at P43212'''<br /> | ||
| - | == | + | ==Crystal Structure of IPP isomerase at P43212== |
| - | + | <StructureSection load='1vcg' size='340' side='right'caption='[[1vcg]], [[Resolution|resolution]] 3.02Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1vcg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VCG 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]] 3.02Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1vcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcg OCA], [https://pdbe.org/1vcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vcg RCSB], [https://www.ebi.ac.uk/pdbsum/1vcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcg ProSAT], [https://www.topsan.org/Proteins/RSGI/1vcg TOPSAN]</span></td></tr> | |
| - | [ | + | </table> |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/IDI2_THET2 IDI2_THET2] Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).[HAMAP-Rule:MF_00354]<ref>PMID:17428035</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/vc/1vcg_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=1vcg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus]] | ||
| + | [[Category: Kuramitsu S]] | ||
| + | [[Category: Park S-Y]] | ||
| + | [[Category: Tame RH]] | ||
| + | [[Category: Wada T]] | ||
| + | [[Category: Yokoyama S]] | ||
Current revision
Crystal Structure of IPP isomerase at P43212
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