4ura

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<StructureSection load='4ura' size='340' side='right'caption='[[4ura]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
<StructureSection load='4ura' size='340' side='right'caption='[[4ura]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ura]] 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=4URA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4URA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ura]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4URA 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=LEL:2-(2H-1,2,3-TRIAZOL-4-YL)PYRIDINE-4-CARBOXYLIC+ACID'>LEL</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>
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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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=LEL:2-(2H-1,2,3-TRIAZOL-4-YL)PYRIDINE-4-CARBOXYLIC+ACID'>LEL</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>
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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=4ura FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ura OCA], [http://pdbe.org/4ura PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ura RCSB], [http://www.ebi.ac.uk/pdbsum/4ura PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ura ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ura FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ura OCA], [https://pdbe.org/4ura PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ura RCSB], [https://www.ebi.ac.uk/pdbsum/4ura PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ura ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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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[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 ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Brennan, P E]]
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[[Category: Brennan PE]]
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[[Category: Burgess-Brown, N]]
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[[Category: Burgess-Brown N]]
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[[Category: Crawley, L]]
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[[Category: Crawley L]]
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[[Category: Delft, F von]]
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[[Category: Edwards A]]
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[[Category: Edwards, A]]
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[[Category: England KS]]
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[[Category: England, K S]]
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[[Category: Krojer T]]
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[[Category: Krojer, T]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U]]
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[[Category: Riesebos E]]
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[[Category: Riesebos, E]]
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[[Category: Szykowska A]]
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[[Category: Szykowska, A]]
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[[Category: Vollmar M]]
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[[Category: Vollmar, M]]
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[[Category: Williams E]]
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[[Category: Williams, E]]
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[[Category: Von Delft F]]
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[[Category: Histone demethylase]]
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[[Category: Jumonjic]]
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[[Category: Oxidoreductase]]
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Revision as of 07:33, 29 March 2023

Crystal structure of human JMJD2A in complex with compound 14a

PDB ID 4ura

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