1clm

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[[Image:1clm.png|left|200px]]
 
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{{STRUCTURE_1clm| PDB=1clm | SCENE= }}
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==STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION==
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<StructureSection load='1clm' size='340' side='right'caption='[[1clm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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===STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION===
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== Structural highlights ==
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<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>
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{{ABSTRACT_PUBMED_8453381}}
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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==About this Structure==
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<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>
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[[1clm]] is a 1 chain structure of [[Calmodulin]] with sequence from [http://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].
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/1clm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Calmodulin|Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:008453381</ref><ref group="xtra">PMID:015576568</ref><references group="xtra"/>
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[[Category: Large Structures]]
[[Category: Paramecium tetraurelia]]
[[Category: Paramecium tetraurelia]]
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[[Category: Sundaralingam, M.]]
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[[Category: Sundaralingam M]]
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[[Category: Calcium-binding protein]]
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STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION

PDB ID 1clm

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