2xdp: Difference between revisions

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<StructureSection load='2xdp' size='340' side='right'caption='[[2xdp]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
<StructureSection load='2xdp' size='340' side='right'caption='[[2xdp]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xdp]] is a 1 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=2XDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XDP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xdp]] is a 1 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=2XDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XDP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.56&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdp OCA], [https://pdbe.org/2xdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xdp RCSB], [https://www.ebi.ac.uk/pdbsum/2xdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xdp 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=2xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdp OCA], [https://pdbe.org/2xdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xdp RCSB], [https://www.ebi.ac.uk/pdbsum/2xdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xdp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/KDM4C_HUMAN KDM4C_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.<ref>PMID:16603238</ref>
[https://www.uniprot.org/uniprot/KDM4C_HUMAN KDM4C_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.<ref>PMID:16603238</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Allerston, C]]
[[Category: Allerston C]]
[[Category: Arrowsmith, C]]
[[Category: Arrowsmith C]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Chaikuad, A]]
[[Category: Chaikuad A]]
[[Category: Daniel, M]]
[[Category: Daniel M]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Gileadi C]]
[[Category: Gileadi, C]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Phillips C]]
[[Category: Phillips, C]]
[[Category: Ugochukwu E]]
[[Category: Ugochukwu, E]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Weisbach H]]
[[Category: Weisbach, H]]
[[Category: Yue WW]]
[[Category: Yue, W W]]
[[Category: Von Delft F]]
[[Category: Histone modification]]
[[Category: Oxidoreductase]]

Latest revision as of 10:29, 20 December 2023

Crystal structure of the tudor domain of human JMJD2C

2xdp, resolution 1.56Å

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