2ypd: Difference between revisions

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<StructureSection load='2ypd' size='340' side='right'caption='[[2ypd]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2ypd' size='340' side='right'caption='[[2ypd]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ypd]] 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=2YPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YPD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ypd]] 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=2YPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YPD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMT:2-(ETHYLMERCURI-THIO)-BENZOIC+ACID'>EMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.1&#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;'>[[2ypr|2ypr]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMT:2-(ETHYLMERCURI-THIO)-BENZOIC+ACID'>EMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2ypd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ypd OCA], [https://pdbe.org/2ypd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ypd RCSB], [https://www.ebi.ac.uk/pdbsum/2ypd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ypd 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=2ypd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ypd OCA], [https://pdbe.org/2ypd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ypd RCSB], [https://www.ebi.ac.uk/pdbsum/2ypd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ypd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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).
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Berridge, G]]
[[Category: Berridge G]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Burgess-Brown, N]]
[[Category: Burgess-Brown N]]
[[Category: Coutandin, D]]
[[Category: Coutandin D]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Froese S]]
[[Category: Froese, S]]
[[Category: Goubin S]]
[[Category: Goubin, S]]
[[Category: Johansson C]]
[[Category: Johansson, C]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Strain-Damerell C]]
[[Category: Strain-Damerell, C]]
[[Category: Vollmar M]]
[[Category: Vollmar, M]]
[[Category: Williams E]]
[[Category: Williams, E]]
[[Category: Von Delft F]]
[[Category: Oxidoreductase]]

Latest revision as of 16:38, 30 August 2023

Crystal structure of the Jumonji domain of human Jumonji domain containing 1C proteinCrystal structure of the Jumonji domain of human Jumonji domain containing 1C protein

Structural highlights

2ypd is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

2ypd, resolution 2.10Å

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OCA
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