5fyh

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<StructureSection load='5fyh' size='340' side='right' caption='[[5fyh]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='5fyh' size='340' side='right' caption='[[5fyh]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fyh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FYH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fyh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FYH FirstGlance]. <br>
</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=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">[[5fxv|5fxv]], [[5fxw|5fxw]], [[5fxx|5fxx]], [[5fxz|5fxz]], [[5fy0|5fy0]], [[5fy1|5fy1]], [[5fy4|5fy4]], [[5fy5|5fy5]], [[5fy7|5fy7]], [[5fy8|5fy8]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyi|5fyi]], [[5fym|5fym]], [[5fys|5fys]], [[5fyt|5fyt]], [[5fyu|5fyu]], [[5fyv|5fyv]], [[5fyy|5fyy]], [[5fyz|5fyz]], [[5fz0|5fz0]], [[5fz1|5fz1]], [[5fz3|5fz3]], [[5fz4|5fz4]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fxv|5fxv]], [[5fxw|5fxw]], [[5fxx|5fxx]], [[5fxz|5fxz]], [[5fy0|5fy0]], [[5fy1|5fy1]], [[5fy4|5fy4]], [[5fy5|5fy5]], [[5fy7|5fy7]], [[5fy8|5fy8]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyi|5fyi]], [[5fym|5fym]], [[5fys|5fys]], [[5fyt|5fyt]], [[5fyu|5fyu]], [[5fyv|5fyv]], [[5fyy|5fyy]], [[5fyz|5fyz]], [[5fz0|5fz0]], [[5fz1|5fz1]], [[5fz3|5fz3]], [[5fz4|5fz4]]</td></tr>
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<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=5fyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyh OCA], [http://pdbe.org/5fyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyh RCSB], [http://www.ebi.ac.uk/pdbsum/5fyh PDBsum]</span></td></tr>
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<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=5fyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyh OCA], [http://pdbe.org/5fyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyh RCSB], [http://www.ebi.ac.uk/pdbsum/5fyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[[http://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>
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==See Also==
 
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*[[Jumonji domain-containing protein|Jumonji domain-containing protein]]
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Bountra, C]]
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[[Category: Delft, F Von]]
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[[Category: Delft, F von]]
[[Category: Edwards, A]]
[[Category: Edwards, A]]
[[Category: Johansson, C]]
[[Category: Johansson, C]]

Revision as of 20:32, 24 January 2018

Crystal structure of human JMJD2A in complex with fumarate

5fyh, resolution 2.35Å

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