1clm: Difference between revisions

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-[[Image:1clm.png|left|200px]]
-{{STRUCTURE_1clm|  PDB=1clm  |  SCENE=  }}
+==STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION==
+<StructureSection load='1clm' size='340' side='right'caption='[[1clm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-===STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION===
+== 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>
-{{ABSTRACT_PUBMED_8453381}}
+</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>
+<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>
-==About this Structure==
+<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 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].
+</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==
-*[[Calmodulin|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-<ref group="xtra">PMID:008453381</ref><ref group="xtra">PMID:015576568</ref><references group="xtra"/>
+[[Category: Large Structures]]
 [[Category: Paramecium tetraurelia]]
-[[Category: Sundaralingam, M.]]
+[[Category: Sundaralingam M]]
-[[Category: Calcium-binding protein]]