5fy8

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==Crystal structure of human JMJD2A in complex with D-threo-isocitrate==
==Crystal structure of human JMJD2A in complex with D-threo-isocitrate==
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<StructureSection load='5fy8' size='340' side='right' caption='[[5fy8]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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<StructureSection load='5fy8' size='340' side='right'caption='[[5fy8]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fy8]] 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=5FY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FY8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fy8]] 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=5FY8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FY8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N81:3-CARBOXY-2,3-DIDEOXY-D-ERYTHRO-PENTARIC+ACID'>N81</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N81:3-CARBOXY-2,3-DIDEOXY-D-ERYTHRO-PENTARIC+ACID'>N81</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">[[5fxv|5fxv]], [[5fxw|5fxw]], [[5fxx|5fxx]], [[5fxz|5fxz]], [[5fy0|5fy0]], [[5fy1|5fy1]], [[5fy4|5fy4]], [[5fy5|5fy5]], [[5fy7|5fy7]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyh|5fyh]], [[5fyi|5fyi]], [[5fym|5fym]]</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]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyh|5fyh]], [[5fyi|5fyi]], [[5fym|5fym]]</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=5fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fy8 OCA], [http://pdbe.org/5fy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fy8 RCSB], [http://www.ebi.ac.uk/pdbsum/5fy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fy8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fy8 OCA], [http://pdbe.org/5fy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fy8 RCSB], [http://www.ebi.ac.uk/pdbsum/5fy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fy8 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 3D structures|Jumonji domain-containing protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Bountra, C]]

Revision as of 07:42, 6 May 2020

Crystal structure of human JMJD2A in complex with D-threo-isocitrate

PDB ID 5fy8

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