1ve4: Difference between revisions
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New page: left|200px<br /><applet load="1ve4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ve4, resolution 1.20Å" /> '''ATP-Phosphoribosyltr... |
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== | ==ATP-Phosphoribosyltransferase(hisG) from Thermus thermophilus HB8== | ||
<StructureSection load='1ve4' size='340' side='right'caption='[[1ve4]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
[[ | == Structural highlights == | ||
[[Category: | <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: Thermus thermophilus]] | ||
[[Category: Omi | [[Category: Omi R]] | ||
Latest revision as of 00:02, 28 December 2023
ATP-Phosphoribosyltransferase(hisG) from Thermus thermophilus HB8
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