1hx5: Difference between revisions
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New page: left|200px<br /><applet load="1hx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hx5, resolution 3.50Å" /> '''Crystal structure of... |
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== | ==Crystal structure of M. tuberculosis chaperonin-10== | ||
<StructureSection load='1hx5' size='340' side='right'caption='[[1hx5]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hx5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HX5 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]] 3.5Å</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=1hx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hx5 OCA], [https://pdbe.org/1hx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hx5 RCSB], [https://www.ebi.ac.uk/pdbsum/1hx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hx5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CH10_MYCTU CH10_MYCTU] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580] | |||
== 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/hx/1hx5_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=1hx5 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Chaperonin 3D structures|Chaperonin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Mande SC]] | |||
[[Category: Mande | [[Category: Taneja B]] | ||
[[Category: Taneja | |||
Latest revision as of 09:17, 9 August 2023
Crystal structure of M. tuberculosis chaperonin-10Crystal structure of M. tuberculosis chaperonin-10
Structural highlights
FunctionCH10_MYCTU Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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