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==STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION== | |||
<StructureSection load='1clm' size='340' side='right'caption='[[1clm]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1clm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CLM 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1clm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clm OCA], [https://pdbe.org/1clm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1clm RCSB], [https://www.ebi.ac.uk/pdbsum/1clm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1clm ProSAT]</span></td></tr> | ||
[[1clm]] is a 1 chain structure | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CALM_PARTE CALM_PARTE] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | |||
== 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/cl/1clm_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=1clm ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Calmodulin|Calmodulin]] | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Paramecium tetraurelia]] | [[Category: Paramecium tetraurelia]] | ||
[[Category: Sundaralingam | [[Category: Sundaralingam M]] | ||
Latest revision as of 09:43, 7 February 2024
STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTIONSTRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION
Structural highlights
FunctionCALM_PARTE Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. 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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