This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5fy8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:31, 26 July 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5fy8' size='340' side='right'caption='[[5fy8]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
<StructureSection load='5fy8' size='340' side='right'caption='[[5fy8]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5fy8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FY8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FY8 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5fy8]] 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=5FY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FY8 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N81:3-CARBOXY-2,3-DIDEOXY-D-ERYTHRO-PENTARIC+ACID'>N81</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 2.343&#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]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyh|5fyh]], [[5fyi|5fyi]], [[5fym|5fym]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N81:3-CARBOXY-2,3-DIDEOXY-D-ERYTHRO-PENTARIC+ACID'>N81</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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://proteopedia.org/fgij/fg.htm?mol=5fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fy8 OCA], [http://pdbe.org/5fy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fy8 RCSB], [http://www.ebi.ac.uk/pdbsum/5fy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fy8 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=5fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fy8 OCA], [https://pdbe.org/5fy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fy8 RCSB], [https://www.ebi.ac.uk/pdbsum/5fy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fy8 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==
Line 17: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Arrowsmith, C H]]
+
[[Category: Arrowsmith CH]]
-
[[Category: Bountra, C]]
+
[[Category: Bountra C]]
-
[[Category: Delft, F von]]
+
[[Category: Edwards A]]
-
[[Category: Edwards, A]]
+
[[Category: Johansson C]]
-
[[Category: Johansson, C]]
+
[[Category: Kopec J]]
-
[[Category: Kopec, J]]
+
[[Category: Nowak R]]
-
[[Category: Nowak, R]]
+
[[Category: Oppermann U]]
-
[[Category: Oppermann, U]]
+
[[Category: Szykowska A]]
-
[[Category: Szykowska, A]]
+
[[Category: Von Delft F]]
-
[[Category: Jmjd2a]]
+
-
[[Category: Kdm4a]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Tca intermediate]]
+

Current revision

Crystal structure of human JMJD2A in complex with D-threo-isocitrate

PDB ID 5fy8

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/5fy8"
Personal tools