4d6r: Difference between revisions

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'''Unreleased structure'''
==crystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamide==
 
<StructureSection load='4d6r' size='340' side='right' caption='[[4d6r]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
The entry 4d6r is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4d6r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D6R FirstGlance]. <br>
Authors: Krojer, T., Vollmar, M., Bradley, A., Crawley, L., Szykowska, A., Burgess-Brown, N., Gileadi, C., Johansson, C., Oppermann, U., Bountra, C., Arrowsmith, C.H., Edwards, A., von Delft, F.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IEJ:O-TOLUENESULFONAMIDE'>IEJ</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d6q|4d6q]], [[4d6s|4d6s]]</td></tr>
Description: crystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamide
<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=4d6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d6r RCSB], [http://www.ebi.ac.uk/pdbsum/4d6r PDBsum]</span></td></tr>
</table>
== Function ==
[[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]]
[[Category: Burgess-Brown, N]]
[[Category: Crawley, L]]
[[Category: Delft, F von]]
[[Category: Edwards, A]]
[[Category: Gileadi, C]]
[[Category: Johansson, C]]
[[Category: Krojer, T]]
[[Category: Oppermann, U]]
[[Category: Szykowska, A]]
[[Category: Vollmar, M]]
[[Category: Demethylase/2og]]
[[Category: Flj10251]]
[[Category: Jumonji domain containing 2d]]
[[Category: Kdm4d]]
[[Category: Mgc141909]]
[[Category: Transcription]]

Revision as of 14:04, 24 December 2014

crystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamidecrystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamide

Structural highlights

4d6r is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  1. ↑ Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z, Spooner E, Li E, Zhang G, Colaiacovo M, Shi Y. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell. 2006 May 5;125(3):467-81. Epub 2006 Apr 6. PMID:16603238 doi:10.1016/j.cell.2006.03.028

4d6r, resolution 1.40Å

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