5fzo

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(New page: ==Crystal structure of the catalytic domain of human JmjD1C== <StructureSection load='5fzo' size='340' side='right' caption='5fzo, resolution 1.84&Aring;' scene=''> == ...)
Current revision (13:33, 26 July 2023) (edit) (undo)
 
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==Crystal structure of the catalytic domain of human JmjD1C==
==Crystal structure of the catalytic domain of human JmjD1C==
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<StructureSection load='5fzo' size='340' side='right' caption='[[5fzo]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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<StructureSection load='5fzo' size='340' side='right'caption='[[5fzo]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fzo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FZO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fzo]] 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=5FZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FZO 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=MN:MANGANESE+(II)+ION'>MN</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]] 1.84&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></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=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fym|5fym]], [[5fys|5fys]], [[5fyt|5fyt]], [[5fyu|5fyu]], [[5fyv|5fyv]], [[5fyy|5fyy]], [[5fyz|5fyz]], [[5fz0|5fz0]], [[5fz1|5fz1]], [[5fz3|5fz3]], [[5fz4|5fz4]], [[5fz6|5fz6]], [[5fz7|5fz7]], [[5fz8|5fz8]], [[5fz9|5fz9]], [[5fza|5fza]], [[5fzb|5fzb]], [[5fzc|5fzc]], [[5fzd|5fzd]], [[5fze|5fze]], [[5fzf|5fzf]], [[5fzg|5fzg]], [[5fzh|5fzh]], [[5fzi|5fzi]], [[5fzk|5fzk]], [[5fzl|5fzl]], [[5fzm|5fzm]]</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=5fzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzo OCA], [https://pdbe.org/5fzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fzo RCSB], [https://www.ebi.ac.uk/pdbsum/5fzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzo ProSAT]</span></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=5fzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzo OCA], [http://pdbe.org/5fzo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fzo RCSB], [http://www.ebi.ac.uk/pdbsum/5fzo PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/JHD2C_HUMAN JHD2C_HUMAN]] Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity).
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[https://www.uniprot.org/uniprot/JHD2C_HUMAN JHD2C_HUMAN] Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity).
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==See Also==
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*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fairhead, M]]
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[[Category: Homo sapiens]]
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[[Category: Goubin, S]]
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[[Category: Large Structures]]
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[[Category: Johansson, C]]
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[[Category: Fairhead M]]
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[[Category: Krojer, T]]
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[[Category: Goubin S]]
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[[Category: McDonough, M]]
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[[Category: Johansson C]]
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[[Category: Nowak, R]]
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[[Category: Krojer T]]
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[[Category: Oppermann, U]]
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[[Category: McDonough M]]
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[[Category: Talon, R]]
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[[Category: Nowak R]]
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[[Category: Jmjd1c]]
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[[Category: Oppermann U]]
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[[Category: Oxidoreductase]]
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[[Category: Talon R]]

Current revision

Crystal structure of the catalytic domain of human JmjD1C

PDB ID 5fzo

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