2xdp
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xdp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XDP FirstGlance]. <br> | <table><tr><td colspan='2'>[[2xdp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XDP FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xdp RCSB], [http://www.ebi.ac.uk/pdbsum/2xdp PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xdp RCSB], [http://www.ebi.ac.uk/pdbsum/2xdp PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/KDM4C_HUMAN KDM4C_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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/chain_selection.php?pdb_ID=2ata ConSurf]. | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Allerston, C | + | [[Category: Allerston, C]] |
- | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C]] |
- | [[Category: Bountra, C | + | [[Category: Bountra, C]] |
- | [[Category: Chaikuad, A | + | [[Category: Chaikuad, A]] |
- | [[Category: Daniel, M | + | [[Category: Daniel, M]] |
- | [[Category: Delft, F Von | + | [[Category: Delft, F Von]] |
- | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
- | [[Category: Gileadi, C | + | [[Category: Gileadi, C]] |
- | [[Category: Krojer, T | + | [[Category: Krojer, T]] |
- | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
- | [[Category: Phillips, C | + | [[Category: Phillips, C]] |
- | [[Category: Ugochukwu, E | + | [[Category: Ugochukwu, E]] |
- | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
- | [[Category: Weisbach, H | + | [[Category: Weisbach, H]] |
- | [[Category: Yue, W W | + | [[Category: Yue, W W]] |
[[Category: Histone modification]] | [[Category: Histone modification]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] |
Revision as of 12:48, 25 December 2014
Crystal structure of the tudor domain of human JMJD2C
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