1cfd
From Proteopedia
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==CALCIUM-FREE CALMODULIN== | ==CALCIUM-FREE CALMODULIN== | ||
- | <StructureSection load='1cfd' size='340' side='right' caption='[[1cfd | + | <StructureSection load='1cfd' size='340' side='right'caption='[[1cfd]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1cfd]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1cfd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The August 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Calmodulin'' by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_8 10.2210/rcsb_pdb/mom_2003_8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFD FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfd OCA], [https://pdbe.org/1cfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfd RCSB], [https://www.ebi.ac.uk/pdbsum/1cfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfd ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/1cfd_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/1cfd_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1cfd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1cfd" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Calmodulin]] | [[Category: Calmodulin]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
- | [[Category: Bax | + | [[Category: Bax A]] |
- | [[Category: Grzesiek | + | [[Category: Grzesiek S]] |
- | [[Category: Klee | + | [[Category: Klee CB]] |
- | [[Category: Kuboniwa | + | [[Category: Kuboniwa H]] |
- | [[Category: Ren | + | [[Category: Ren H]] |
- | [[Category: Tjandra | + | [[Category: Tjandra N]] |
- | + |
Current revision
CALCIUM-FREE CALMODULIN
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