4aap
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4aap]] 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=4AAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AAP FirstGlance]. <br> | <table><tr><td colspan='2'>[[4aap]] 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=4AAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AAP FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </span></td></tr> |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4aap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aap OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aap RCSB], [http://www.ebi.ac.uk/pdbsum/4aap PDBsum]</span></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=4aap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aap OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aap RCSB], [http://www.ebi.ac.uk/pdbsum/4aap PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/KDM8_HUMAN KDM8_HUMAN]] Histone demethylase required for G2/M phase cell cycle progression. Specifically demethylates dimethylated 'Lys-36' (H3K36me2) of histone H3, an epigenetic repressive mark, thereby acting as a transcription activator. Regulates expression of CCNA1 (cyclin-A1), leading to regulate cancer cell proliferation. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Allerston, C | + | [[Category: Allerston, C]] |
- | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
- | [[Category: Bountra, C | + | [[Category: Bountra, C]] |
- | [[Category: Canning, P | + | [[Category: Canning, P]] |
- | [[Category: Delft, F Von | + | [[Category: Delft, F Von]] |
- | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
- | [[Category: Gadhave, A | + | [[Category: Gadhave, A]] |
- | [[Category: Johansson, C | + | [[Category: Johansson, C]] |
- | [[Category: Krojer, T | + | [[Category: Krojer, T]] |
- | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
- | [[Category: Vollmar, M | + | [[Category: Vollmar, M]] |
- | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] |
Revision as of 02:10, 25 December 2014
Crystal structure of JMJD5 domain of human Lysine-specific demethylase 8 (KDM8) in complex with N-oxalylglycine (NOG)
|