1clm: Difference between revisions

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{{Seed}}
[[Image:1clm.png|left|200px]]


<!--
==STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_1clm", creates the "Structure Box" on the page.
<StructureSection load='1clm' size='340' side='right'caption='[[1clm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1clm| PDB=1clm |  SCENE= }}
<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>
</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>


===STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION===
==See Also==
 
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 
__TOC__
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</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_8453381}}, adds the Publication Abstract to the page
[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 8453381 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8453381}}
 
==About this Structure==
1CLM is a 1 chain structure of 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].
 
==Reference==
<ref group="xtra">PMID:8453381</ref><references group="xtra"/>
[[Category: Paramecium tetraurelia]]
[[Category: Paramecium tetraurelia]]
[[Category: Sundaralingam, M.]]
[[Category: Sundaralingam M]]
[[Category: Calcium-binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:46:34 2009''

Latest revision as of 06:43, 7 February 2024

STRUCTURE OF PARAMECIUM TETRAURELIA CALMODULIN AT 1.8 ANGSTROMS RESOLUTION

1clm, resolution 1.80Å

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