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.


5kr7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:52, 27 September 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5kr7' size='340' side='right'caption='[[5kr7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5kr7' size='340' side='right'caption='[[5kr7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5kr7]] 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=5KR7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KR7 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5kr7]] 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=5KR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KR7 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6X9:6-ETHYL-2,5-DIMETHYL-7-OXIDANYLIDENE-4~{H}-PYRAZOLO[1,5-A]PYRIMIDINE-3-CARBONITRILE'>6X9</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 1.9&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KDM4C, GASC1, JHDM3C, JMJD2C, KIAA0780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6X9:6-ETHYL-2,5-DIMETHYL-7-OXIDANYLIDENE-4~{H}-PYRAZOLO[1,5-A]PYRIMIDINE-3-CARBONITRILE'>6X9</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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'>[http://proteopedia.org/fgij/fg.htm?mol=5kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kr7 OCA], [http://pdbe.org/5kr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kr7 RCSB], [http://www.ebi.ac.uk/pdbsum/5kr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kr7 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=5kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kr7 OCA], [https://pdbe.org/5kr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kr7 RCSB], [https://www.ebi.ac.uk/pdbsum/5kr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kr7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/KDM4C_HUMAN KDM4C_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.<ref>PMID:16603238</ref>
+
[https://www.uniprot.org/uniprot/KDM4C_HUMAN KDM4C_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.<ref>PMID:16603238</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 26: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Bellon, S F]]
+
[[Category: Bellon SF]]
-
[[Category: Poy, F]]
+
[[Category: Poy F]]
-
[[Category: Setser, J W]]
+
[[Category: Setser JW]]
-
[[Category: Histone]]
+
-
[[Category: Inhibitor]]
+
-
[[Category: Lysine demethylase]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

KDM4C bound to pyrazolo-pyrimidine scaffold

PDB ID 5kr7

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/5kr7"
Personal tools