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.


6ete

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:21, 9 May 2024) (edit) (undo)
 
Line 1: Line 1:
==Crystal structure of KDM4D with tetrazolhydrazide compound 5==
==Crystal structure of KDM4D with tetrazolhydrazide compound 5==
-
<StructureSection load='6ete' size='340' side='right' caption='[[6ete]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
+
<StructureSection load='6ete' size='340' side='right'caption='[[6ete]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6ete]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ETE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ETE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6ete]] is a 1 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=6ETE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ETE FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BWK:[2-(1-methyl-1,2,3,4-tetrazol-4-ium-5-yl)ethanoylamino]azanium'>BWK</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 1.468&#8491;</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=6ete FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ete OCA], [http://pdbe.org/6ete PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ete RCSB], [http://www.ebi.ac.uk/pdbsum/6ete PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ete ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BWK:[2-(1-methyl-1,2,3,4-tetrazol-4-ium-5-yl)ethanoylamino]azanium'>BWK</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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'>[https://proteopedia.org/fgij/fg.htm?mol=6ete FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ete OCA], [https://pdbe.org/6ete PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ete RCSB], [https://www.ebi.ac.uk/pdbsum/6ete PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ete ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref>
+
[https://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref>
 +
 
 +
==See Also==
 +
*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
 +
*[[Lysine-specific histone demethylase 3D structures|Lysine-specific histone demethylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Heinemann, U]]
+
[[Category: Homo sapiens]]
-
[[Category: Link, A]]
+
[[Category: Large Structures]]
-
[[Category: Malecki, P H]]
+
[[Category: Heinemann U]]
-
[[Category: Weiss, M S]]
+
[[Category: Link A]]
-
[[Category: Cancer]]
+
[[Category: Malecki PH]]
-
[[Category: Epigenetic]]
+
[[Category: Weiss MS]]
-
[[Category: Inhibitor design]]
+
-
[[Category: Kdm4d]]
+
-
[[Category: Ligand binding]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Tetrazole]]
+
-
[[Category: Tetrazolylhydrazide]]
+

Current revision

Crystal structure of KDM4D with tetrazolhydrazide compound 5

PDB ID 6ete

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools