5a7p: Difference between revisions

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<StructureSection load='5a7p' size='340' side='right'caption='[[5a7p]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
<StructureSection load='5a7p' size='340' side='right'caption='[[5a7p]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5a7p]] 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=5A7P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A7P FirstGlance]. <br>
<table><tr><td colspan='2'>[[5a7p]] 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=5A7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A7P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6Z1:2-[5-[(5-METHYL-1,2-OXAZOL-3-YL)CARBONYLAMINO]-2-OXIDANYL-PHENYL]PYRIDINE-4-CARBOXYLIC+ACID'>6Z1</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a7n|5a7n]], [[5a7o|5a7o]], [[5a7q|5a7q]], [[5a7s|5a7s]], [[5a7w|5a7w]], [[5a80|5a80]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6Z1:2-[5-[(5-METHYL-1,2-OXAZOL-3-YL)CARBONYLAMINO]-2-OXIDANYL-PHENYL]PYRIDINE-4-CARBOXYLIC+ACID'>6Z1</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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='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=5a7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a7p OCA], [http://pdbe.org/5a7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a7p RCSB], [http://www.ebi.ac.uk/pdbsum/5a7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a7p ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a7p OCA], [https://pdbe.org/5a7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a7p RCSB], [https://www.ebi.ac.uk/pdbsum/5a7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a7p 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>
[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>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Froese S]]
[[Category: Froese, S]]
[[Category: Fujimori DG]]
[[Category: Fujimori, D G]]
[[Category: Gileadi C]]
[[Category: Gileadi, C]]
[[Category: Gregori-Puigjane E]]
[[Category: Gregori-Puigjane, E]]
[[Category: Iwasa E]]
[[Category: Iwasa, E]]
[[Category: Johansson C]]
[[Category: Johansson, C]]
[[Category: Kopec J]]
[[Category: Kopec, J]]
[[Category: Korczynska M]]
[[Category: Korczynska, M]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Le DD]]
[[Category: Le, D D]]
[[Category: Nowak R]]
[[Category: Nowak, R]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Ortiz Torres I]]
[[Category: Pollock, S B]]
[[Category: Pollock SB]]
[[Category: Shoichet, B K]]
[[Category: Shoichet BK]]
[[Category: Tallant, C]]
[[Category: Tallant C]]
[[Category: Torres, I Ortiz]]
[[Category: Tumber A]]
[[Category: Tumber, A]]
[[Category: Velupillai S]]
[[Category: Velupillai, S]]
[[Category: Younger N]]
[[Category: Younger, N]]
[[Category: Von Delft F]]
[[Category: Jmjd2a]]
[[Category: Kdm4a]]
[[Category: Oxidoreductase]]

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