5f5a: Difference between revisions
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''' | ==Crystal Structure of human JMJD2D complexed with KDOAM16== | ||
<StructureSection load='5f5a' size='340' side='right' caption='[[5f5a]], [[Resolution|resolution]] 1.41Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f5a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F5A FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5V0:2-[(FURAN-2-YLMETHYLAMINO)METHYL]PYRIDINE-4-CARBOXYLIC+ACID'>5V0</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5f5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5a OCA], [http://pdbe.org/5f5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f5a RCSB], [http://www.ebi.ac.uk/pdbsum/5f5a PDBsum]</span></td></tr> | |||
</table> | |||
[[Category: | == Function == | ||
[[Category: | [[http://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arrowsmith, C H]] | |||
[[Category: Bountra, C]] | |||
[[Category: Bradley, A R]] | |||
[[Category: Brennan, P]] | |||
[[Category: Burgess-Brown, N]] | [[Category: Burgess-Brown, N]] | ||
[[Category: | [[Category: Burley, S K]] | ||
[[Category: Crawley, L]] | |||
[[Category: Delft, F von]] | |||
[[Category: Edwards, A]] | |||
[[Category: Krojer, T]] | [[Category: Krojer, T]] | ||
[[Category: Oppermann, U]] | [[Category: Oppermann, U]] | ||
[[Category: Ruda, G F]] | |||
[[Category: Structural genomic]] | |||
[[Category: Szykowska, A]] | [[Category: Szykowska, A]] | ||
[[Category: | [[Category: Vollmar, M]] | ||
[[Category: | [[Category: Yang, H]] | ||
[[Category: | [[Category: Demethylase]] | ||
[[Category: | [[Category: Double-stranded beta helix]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Oxygenase]] | ||
[[Category: Sgc]] |
Revision as of 16:59, 16 December 2015
Crystal Structure of human JMJD2D complexed with KDOAM16Crystal Structure of human JMJD2D complexed with KDOAM16
Structural highlights
Function[KDM4D_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.[1] References
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