5fyh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5fyh" [edit=sysop:move=sysop])
Current revision (13:31, 26 July 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of human JMJD2A in complex with fumarate==
==Crystal structure of human JMJD2A in complex with fumarate==
-
<StructureSection load='5fyh' size='340' side='right' caption='[[5fyh]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+
<StructureSection load='5fyh' size='340' side='right'caption='[[5fyh]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5fyh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FYH FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5fyh]] 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=5FYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FYH FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.348&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fxv|5fxv]], [[5fxw|5fxw]], [[5fxx|5fxx]], [[5fxz|5fxz]], [[5fy0|5fy0]], [[5fy1|5fy1]], [[5fy4|5fy4]], [[5fy5|5fy5]], [[5fy7|5fy7]], [[5fy8|5fy8]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyi|5fyi]], [[5fym|5fym]], [[5fys|5fys]], [[5fyt|5fyt]], [[5fyu|5fyu]], [[5fyv|5fyv]], [[5fyy|5fyy]], [[5fyz|5fyz]], [[5fz0|5fz0]], [[5fz1|5fz1]], [[5fz3|5fz3]], [[5fz4|5fz4]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyh OCA], [http://pdbe.org/5fyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyh RCSB], [http://www.ebi.ac.uk/pdbsum/5fyh PDBsum]</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=5fyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyh OCA], [https://pdbe.org/5fyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fyh RCSB], [https://www.ebi.ac.uk/pdbsum/5fyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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>
+
[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>
==See Also==
==See Also==
-
*[[Jumonji domain-containing protein|Jumonji domain-containing protein]]
+
*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Arrowsmith, C H]]
+
[[Category: Homo sapiens]]
-
[[Category: Bountra, C]]
+
[[Category: Large Structures]]
-
[[Category: Delft, F Von]]
+
[[Category: Arrowsmith CH]]
-
[[Category: Edwards, A]]
+
[[Category: Bountra C]]
-
[[Category: Johansson, C]]
+
[[Category: Edwards A]]
-
[[Category: Kopec, J]]
+
[[Category: Johansson C]]
-
[[Category: Nowak, R]]
+
[[Category: Kopec J]]
-
[[Category: Oppermann, U]]
+
[[Category: Nowak R]]
-
[[Category: Szykowska, A]]
+
[[Category: Oppermann U]]
-
[[Category: Jmjd2a]]
+
[[Category: Szykowska A]]
-
[[Category: Kdm4a]]
+
[[Category: Von Delft F]]
-
[[Category: Oxidoreductase]]
+
-
[[Category: Tca intermediate]]
+

Current revision

Crystal structure of human JMJD2A in complex with fumarate

PDB ID 5fyh

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/5fyh"
Personal tools