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==CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE== | ==CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE== | ||
<StructureSection load='1i0e' size='340' side='right' caption='[[1i0e]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1i0e' size='340' side='right'caption='[[1i0e]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1i0e]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1i0e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I0E FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
<tr><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=1i0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i0e OCA], [https://pdbe.org/1i0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i0e RCSB], [https://www.ebi.ac.uk/pdbsum/1i0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i0e ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/KCRM_HUMAN KCRM_HUMAN] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. | |||
== 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/i0/1i0e_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i0/1i0e_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> | ||
</jmolCheckbox> | </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/ | </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=1i0e ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Creatine | *[[Creatine kinase 3D structures|Creatine kinase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lin | [[Category: Large Structures]] | ||
[[Category: Shen | [[Category: Lin Z-J]] | ||
[[Category: Tang | [[Category: Shen Y-Q]] | ||
[[Category: Zhou | [[Category: Tang L]] | ||
[[Category: Zhou H-M]] | |||
Latest revision as of 16:24, 13 March 2024
CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLECRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE
Structural highlights
FunctionKCRM_HUMAN Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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