2ybk
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ybk' size='340' side='right'caption='[[2ybk]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2ybk' size='340' side='right'caption='[[2ybk]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ybk]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ybk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YBK FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HG:(2R)-2-HYDROXYPENTANEDIOIC+ACID'>2HG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HG:(2R)-2-HYDROXYPENTANEDIOIC+ACID'>2HG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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">[[2wwj|2wwj]], [[2gfa|2gfa]], [[2vd7|2vd7]], [[2ybs|2ybs]], [[2ybp|2ybp]], [[2gp3|2gp3]], [[2gf7|2gf7]], [[2gp5|2gp5]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wwj|2wwj]], [[2gfa|2gfa]], [[2vd7|2vd7]], [[2ybs|2ybs]], [[2ybp|2ybp]], [[2gp3|2gp3]], [[2gf7|2gf7]], [[2gp5|2gp5]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ybk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybk OCA], [https://pdbe.org/2ybk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ybk RCSB], [https://www.ebi.ac.uk/pdbsum/2ybk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ybk ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 05:25, 10 August 2022
JMJD2A COMPLEXED WITH R-2-HYDROXYGLUTARATE
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Categories: Human | Large Structures | Chowdhury, R | McDonough, M A | Schofield, C J | 2-oxoglutarate | Chromatin regulator | Dioxygenase | Double-stranded beta helix | Dsbh | Epigenetic and transcription regulation | Facial triad | Hydroxylation | Iron | Metal binding protein | Non-heme | Oxidoreductase | Oxygenase
