3ifk: Difference between revisions

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'''Unreleased structure'''


The entry 3ifk is ON HOLD
==Crystal Structure Of Calcium-Saturated Calmodulin N-terminal Domain Fragment, Residues 1-90==
<StructureSection load='3ifk' size='340' side='right'caption='[[3ifk]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ifk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IFK 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]] 2.03&#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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ifk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ifk OCA], [https://pdbe.org/3ifk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ifk RCSB], [https://www.ebi.ac.uk/pdbsum/3ifk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ifk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]
== 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/if/3ifk_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=3ifk ConSurf].
<div style="clear:both"></div>


Authors: Witt, T.J., Newman, R.A., Shea, M.A.
==See Also==
 
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
Description: Crystal Structure Of Calcium-Saturated Calmodulin N-terminal Domain Fragment, Residues 1-90
__TOC__
 
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 12 12:25:24 2009''
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Newman RA]]
[[Category: Shea MA]]
[[Category: Witt TJ]]

Latest revision as of 13:05, 21 February 2024

Crystal Structure Of Calcium-Saturated Calmodulin N-terminal Domain Fragment, Residues 1-90Crystal Structure Of Calcium-Saturated Calmodulin N-terminal Domain Fragment, Residues 1-90

Structural highlights

3ifk is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.03Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CALM1_RAT Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3ifk, resolution 2.03Å

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