2gp5: Difference between revisions

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-[[Image:2gp5.png|left|200px]]
-{{STRUCTURE_2gp5|  PDB=2gp5  |  SCENE=  }}
+==Crystal structure of catalytic core domain of jmjd2A complexed with alpha-Ketoglutarate==
+<StructureSection load='2gp5' size='340' side='right'caption='[[2gp5]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2gp5]] 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=2GP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GP5 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]] 2.28&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2gp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gp5 OCA], [https://pdbe.org/2gp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gp5 RCSB], [https://www.ebi.ac.uk/pdbsum/2gp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gp5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_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. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref>   Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/2gp5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gp5 ConSurf].
+<div style="clear:both"></div>
-===Crystal structure of catalytic core domain of jmjd2A complexed with alpha-Ketoglutarate===
+==See Also==
+*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
-{{ABSTRACT_PUBMED_16677698}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[2gp5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GP5 OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:016677698</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Chen, Z.]]
+[[Category: Large Structures]]
-[[Category: Dai, S.]]
+[[Category: Chen Z]]
-[[Category: Davrazou, F.]]
+[[Category: Dai S]]
-[[Category: Hagman, J.]]
+[[Category: Davrazou F]]
-[[Category: Hong, X.]]
+[[Category: Hagman J]]
-[[Category: Kutateladze, T G.]]
+[[Category: Hong X]]
-[[Category: Shi, Y.]]
+[[Category: Kutateladze TG]]
-[[Category: Simpson, M.]]
+[[Category: Shi Y]]
-[[Category: Whetstine, J.]]
+[[Category: Simpson M]]
-[[Category: Zang, J.]]
+[[Category: Whetstine J]]
-[[Category: Zhang, G.]]
+[[Category: Zang J]]
-[[Category: Beta barrel]]
+[[Category: Zhang G]]
-[[Category: Metal binding protein]]
-[[Category: Zinc finger]]