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5fp7

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==Crystal structure of human KDM4D in complex with 3-4-methylthiophen-2- yl methylaminopyridine-4-carboxylic acid==
==Crystal structure of human KDM4D in complex with 3-4-methylthiophen-2- yl methylaminopyridine-4-carboxylic acid==
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<StructureSection load='5fp7' size='340' side='right' caption='[[5fp7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='5fp7' size='340' side='right'caption='[[5fp7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fp7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FP7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fp7]] 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=5FP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FP7 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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YC8:3-(4-PHENYLBUTANOYLAMINO)PYRIDINE-4-CARBOXYLIC+ACID'>YC8</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fp3|5fp3]], [[5fp4|5fp4]], [[5fp8|5fp8]], [[5fp9|5fp9]], [[5fpa|5fpa]], [[5fpb|5fpb]]</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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YC8:3-(4-PHENYLBUTANOYLAMINO)PYRIDINE-4-CARBOXYLIC+ACID'>YC8</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=5fp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fp7 OCA], [http://pdbe.org/5fp7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fp7 RCSB], [http://www.ebi.ac.uk/pdbsum/5fp7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fp7 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=5fp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fp7 OCA], [https://pdbe.org/5fp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fp7 RCSB], [https://www.ebi.ac.uk/pdbsum/5fp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fp7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref>
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[https://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5fp7" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5fp7" style="background-color:#fffaf0;"></div>
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==See Also==
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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: Chung, C]]
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[[Category: Homo sapiens]]
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[[Category: Inhibitor]]
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[[Category: Large Structures]]
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[[Category: Jmjd2d]]
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[[Category: Chung C]]
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[[Category: Jumonji]]
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[[Category: Kdm4d]]
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[[Category: Lysine specific histone demethylase]]
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Current revision

Crystal structure of human KDM4D in complex with 3-4-methylthiophen-2- yl methylaminopyridine-4-carboxylic acid

PDB ID 5fp7

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