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2xml

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==Crystal structure of human JMJD2C catalytic domain==
==Crystal structure of human JMJD2C catalytic domain==
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<StructureSection load='2xml' size='340' side='right' caption='[[2xml]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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<StructureSection load='2xml' size='340' side='right'caption='[[2xml]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xml]] 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=2XML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XML FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xml]] 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=2XML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XML 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdp|2xdp]]</td></tr>
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<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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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=2xml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xml OCA], [http://pdbe.org/2xml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xml RCSB], [http://www.ebi.ac.uk/pdbsum/2xml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xml 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=2xml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xml OCA], [https://pdbe.org/2xml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xml RCSB], [https://www.ebi.ac.uk/pdbsum/2xml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xml ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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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==See Also==
==See Also==
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*[[Jumonji domain-containing protein|Jumonji domain-containing protein]]
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*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C]]
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[[Category: Large Structures]]
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[[Category: Bountra, C]]
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[[Category: Arrowsmith C]]
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[[Category: Carpenter, L]]
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[[Category: Bountra C]]
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[[Category: Delft, F von]]
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[[Category: Carpenter L]]
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[[Category: Edwards, A]]
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[[Category: Edwards A]]
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[[Category: Gileadi, C]]
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[[Category: Gileadi C]]
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[[Category: Krojer, T]]
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[[Category: Krojer T]]
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[[Category: Ng, S]]
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[[Category: Ng S]]
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[[Category: Oppermann, U]]
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[[Category: Oppermann U]]
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[[Category: Pike, A C.W]]
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[[Category: Pike ACW]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Yue, W W]]
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[[Category: Yue WW]]
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[[Category: Metal binding]]
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[[Category: Von Delft F]]
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[[Category: Oxidoreductase]]
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[[Category: Transcription regulation]]
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Current revision

Crystal structure of human JMJD2C catalytic domain

PDB ID 2xml

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