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2heh
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2heh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2heh, resolution 2.15Å" /> '''Crystal Structure o...) |
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| - | [[Image:2heh.gif|left|200px]]<br /> | ||
| - | <applet load="2heh" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2heh, resolution 2.15Å" /> | ||
| - | '''Crystal Structure of the KIF2C motor domain (CASP Target)'''<br /> | ||
| - | == | + | ==Crystal Structure of the KIF2C motor domain== |
| - | + | <StructureSection load='2heh' size='340' side='right'caption='[[2heh]], [[Resolution|resolution]] 2.15Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2heh]] is a 1 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=2HEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HEH 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]] 2.15Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2heh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2heh OCA], [https://pdbe.org/2heh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2heh RCSB], [https://www.ebi.ac.uk/pdbsum/2heh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2heh ProSAT]</span></td></tr> |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/KIF2C_HUMAN KIF2C_HUMAN] In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis.<ref>PMID:19060894</ref> <ref>PMID:21820309</ref> | |
| - | [ | + | == 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/he/2heh_consurf.spt"</scriptWhenChecked> |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2heh ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
| - | [ | + | |
| - | [[ | + | |
| - | [ | + | |
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Kinesin 3D Structures|Kinesin 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith CH]] | ||
| + | [[Category: Bochkarev A]] | ||
| + | [[Category: Edwards AM]] | ||
| + | [[Category: Landry R]] | ||
| + | [[Category: Park H]] | ||
| + | [[Category: Shen Y]] | ||
| + | [[Category: Sundstrom M]] | ||
| + | [[Category: Tempel W]] | ||
| + | [[Category: Wang J]] | ||
| + | [[Category: Weigelt J]] | ||
Current revision
Crystal Structure of the KIF2C motor domain
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bochkarev A | Edwards AM | Landry R | Park H | Shen Y | Sundstrom M | Tempel W | Wang J | Weigelt J
