5f5c: Difference between revisions

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'''Unreleased structure'''
==Crystal Structure of human JMJD2D complexed with KDOPP7==
 
<StructureSection load='5f5c' size='340' side='right' caption='[[5f5c]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
The entry 5f5c is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5f5c]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F5C FirstGlance]. <br>
Authors: Krojer, T., Vollmar, M., Crawley, L., Bradley, A.R., Szykowska, A., Ruda, G.F., Yang, H., Burgess-Brown, N., Brennan, P., Burley, S.K., Bountra, C., Arrowsmith, C.H., Edwards, A., Oppermann, U., von Delft, F., Structural Genomics Consortium (SGC)
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5V3:8-[[(PHENYLMETHYL)AMINO]METHYL]-1~{H}-PYRIDO[3,4-D]PYRIMIDIN-4-ONE'>5V3</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=5f5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5c OCA], [http://pdbe.org/5f5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f5c RCSB], [http://www.ebi.ac.uk/pdbsum/5f5c PDBsum]</span></td></tr>
Description: Crystal Structure of human JMJD2D complexed with KDOPP7
</table>
[[Category: Unreleased Structures]]
== Function ==
[[Category: Ruda, G.F]]
[[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: Yang, H]]
[[Category: Burley, S K]]
[[Category: Crawley, L]]
[[Category: Delft, F von]]
[[Category: Edwards, A]]
[[Category: Krojer, T]]
[[Category: Krojer, T]]
[[Category: Bountra, C]]
[[Category: Vollmar, M]]
[[Category: Burley, S.K]]
[[Category: Arrowsmith, C.H]]
[[Category: Oppermann, U]]
[[Category: Oppermann, U]]
[[Category: Ruda, G F]]
[[Category: Structural genomic]]
[[Category: Szykowska, A]]
[[Category: Szykowska, A]]
[[Category: Crawley, L]]
[[Category: Vollmar, M]]
[[Category: Von Delft, F]]
[[Category: Yang, H]]
[[Category: Bradley, A.R]]
[[Category: Demethylase]]
[[Category: Structural Genomics Consortium (Sgc)]]
[[Category: Double-stranded beta helix]]
[[Category: Edwards, A]]
[[Category: Oxidoreductase]]
[[Category: Brennan, P]]
[[Category: Oxygenase]]
[[Category: Sgc]]
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