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6ax3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Complex structure of JMJD5 and Symmetric Dimethyl-Arginine (SDMA)== | |
| - | + | <StructureSection load='6ax3' size='340' side='right' caption='[[6ax3]], [[Resolution|resolution]] 2.25Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ax3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AX3 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2MR:N3,+N4-DIMETHYLARGININE'>2MR</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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 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=6ax3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ax3 OCA], [http://pdbe.org/6ax3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ax3 RCSB], [http://www.ebi.ac.uk/pdbsum/6ax3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ax3 ProSAT]</span></td></tr> |
| + | </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__ | ||
| + | </StructureSection> | ||
[[Category: Dai, S]] | [[Category: Dai, S]] | ||
| + | [[Category: Lee, S]] | ||
[[Category: Liu, H]] | [[Category: Liu, H]] | ||
| - | [[Category: | + | [[Category: Wang, Y]] |
[[Category: Zhang, G]] | [[Category: Zhang, G]] | ||
| + | [[Category: Demethylase]] | ||
| + | [[Category: Endopeptidase]] | ||
| + | [[Category: Exopeptidase]] | ||
| + | [[Category: Histone]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Jumonji]] | ||
Revision as of 06:30, 28 February 2018
Complex structure of JMJD5 and Symmetric Dimethyl-Arginine (SDMA)
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Categories: Dai, S | Lee, S | Liu, H | Wang, Y | Zhang, G | Demethylase | Endopeptidase | Exopeptidase | Histone | Hydrolase | Jumonji
