3pdq: Difference between revisions

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<StructureSection load='3pdq' size='340' side='right'caption='[[3pdq]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='3pdq' size='340' side='right'caption='[[3pdq]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3pdq]] 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=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3pdq]] 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=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 1.989&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3njy|3njy]], [[2wwj|2wwj]], [[2vd7|2vd7]], [[2oq7|2oq7]], [[2ox0|2ox0]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KDM4A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [https://pdbe.org/3pdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [https://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq 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=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [https://pdbe.org/3pdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [https://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq 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>
[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>  


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chang, K H]]
[[Category: Chang K-H]]
[[Category: Clifton, I J]]
[[Category: Clifton IJ]]
[[Category: King, O N.F]]
[[Category: King ONF]]
[[Category: McDonough, M A]]
[[Category: McDonough MA]]
[[Category: Rose, N R]]
[[Category: Rose NR]]
[[Category: Schofield, C J]]
[[Category: Schofield CJ]]
[[Category: 2-oxoglutarate]]
[[Category: Alpha-ketoglutarate]]
[[Category: Chromatin regulator]]
[[Category: Demethylation]]
[[Category: Dioxygenase]]
[[Category: Iron]]
[[Category: Jmjc domain]]
[[Category: Nucleus]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Transcription]]
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