6f5r
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6f5r is ON HOLD Authors: Malecki, P.H., Link, A., Weiss, M.S., Heinemann, U. Description: Crystal Structure of KDM4D with GF028 ligand [[Category: ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of KDM4D with GF028 ligand== | |
| - | + | <StructureSection load='6f5r' size='340' side='right' caption='[[6f5r]], [[Resolution|resolution]] 1.61Å' scene=''> | |
| - | + | == 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> | |
| - | + | </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: | + | <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: Link, A]] | [[Category: Link, A]] | ||
| - | [[Category: | + | [[Category: Malecki, P H]] |
| - | [[Category: Weiss, M | + | [[Category: Weiss, M S]] |
| - | [[Category: | + | [[Category: Cancer]] |
| + | [[Category: Drug development]] | ||
| + | [[Category: Epigenetic]] | ||
| + | [[Category: Inhibitor design]] | ||
| + | [[Category: Kdm4 ligand binding]] | ||
| + | [[Category: Kdm4d]] | ||
| + | [[Category: Ligand optimization]] | ||
| + | [[Category: Oxidoreductase]] | ||
Current revision
Crystal Structure of KDM4D with GF028 ligand
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