6f5r: Difference between revisions

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'''Unreleased structure'''


The entry 6f5r is ON HOLD  until Paper Publication
==Crystal Structure of KDM4D with GF028 ligand==
 
<StructureSection load='6f5r' size='340' side='right' caption='[[6f5r]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
Authors: Malecki, P.H., Link, A., Weiss, M.S., Heinemann, U.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6f5r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F5R FirstGlance]. <br>
Description: Crystal Structure of KDM4D with GF028 ligand
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CQZ:2-(3-oxidanylpropylamino)pyridine-4-carboxylic+acid'>CQZ</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>
[[Category: Unreleased Structures]]
<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=6f5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f5r OCA], [http://pdbe.org/6f5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f5r RCSB], [http://www.ebi.ac.uk/pdbsum/6f5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f5r ProSAT]</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: Heinemann, U]]
[[Category: Heinemann, U]]
[[Category: Malecki, P.H]]
[[Category: Link, A]]
[[Category: Link, A]]
[[Category: Weiss, M.S]]
[[Category: Malecki, P H]]
[[Category: Weiss, M S]]
[[Category: Cancer]]
[[Category: Drug development]]
[[Category: Epigenetic]]
[[Category: Inhibitor design]]
[[Category: Kdm4 ligand binding]]
[[Category: Kdm4d]]
[[Category: Ligand optimization]]
[[Category: Oxidoreductase]]

Latest revision as of 09:49, 12 December 2018

Crystal Structure of KDM4D with GF028 ligandCrystal Structure of KDM4D with GF028 ligand

Structural highlights

6f5r 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, PDBe, RCSB, PDBsum, ProSAT

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

6f5r, resolution 1.61Å

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