1ve4
From Proteopedia
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| - | [[Image:1ve4.gif|left|200px]]<br /><applet load="1ve4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ve4, resolution 1.20Å" /> | ||
| - | '''ATP-Phosphoribosyltransferase(hisG) from Thermus thermophilus HB8'''<br /> | ||
| - | == | + | ==ATP-Phosphoribosyltransferase(hisG) from Thermus thermophilus HB8== |
| - | + | <StructureSection load='1ve4' size='340' side='right'caption='[[1ve4]], [[Resolution|resolution]] 1.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1ve4]] is a 1 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=1VE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VE4 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]] 1.2Å</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=1ve4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve4 OCA], [https://pdbe.org/1ve4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ve4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ve4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve4 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ve4 TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | [ | + | [https://www.uniprot.org/uniprot/HIS1_THET2 HIS1_THET2] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (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/ve/1ve4_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=1ve4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus]] | ||
| + | [[Category: Omi R]] | ||
Current revision
ATP-Phosphoribosyltransferase(hisG) from Thermus thermophilus HB8
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