5kjh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:40, 2 April 2025) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5kjh' size='340' side='right'caption='[[5kjh]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
<StructureSection load='5kjh' size='340' side='right'caption='[[5kjh]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5kjh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5ch1 5ch1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJH FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5kjh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27&#8491;</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]] 2.27&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
Line 9: Line 9:
</table>
</table>
== Function ==
== Function ==
-
[https://www.uniprot.org/uniprot/G0S8H7_CHATD G0S8H7_CHATD]
+
[https://www.uniprot.org/uniprot/EED_CHATD EED_CHATD] Component of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3) (PubMed:26472914, PubMed:29904056). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056). EED is not a catalytic subunit but is required for the complex regulation of histone H3 lysine methylation by EZH2 (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056).<ref>PMID:26472914</ref> <ref>PMID:28008037</ref> <ref>PMID:28607149</ref> <ref>PMID:29904056</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Current revision

Crystal structure of an active polycomb repressive complex 2 in the stimulated state

PDB ID 5kjh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kjh"
Personal tools