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5F59

The crystal structure of MLL3 SET domain

Summary for 5F59
Entry DOI10.2210/pdb5f59/pdb
Related5F5E 5F6K 5F6L
DescriptorHistone-lysine N-methyltransferase 2C, ZINC ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
Functional Keywordshistone methylation, histone methyltransferase, set domain, transferase
Biological sourceHomo sapiens (Human)
Cellular locationNucleus : Q8NEZ4
Total number of polymer chains1
Total formula weight18453.42
Authors
Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-04, release date: 2016-02-24, Last modification date: 2024-03-20)
Primary citationLi, Y.,Han, J.,Zhang, Y.,Cao, F.,Liu, Z.,Li, S.,Wu, J.,Hu, C.,Wang, Y.,Shuai, J.,Chen, J.,Cao, L.,Li, D.,Shi, P.,Tian, C.,Zhang, J.,Dou, Y.,Li, G.,Chen, Y.,Lei, M.
Structural basis for activity regulation of MLL family methyltransferases.
Nature, 530:447-452, 2016
Cited by
PubMed: 26886794
DOI: 10.1038/nature16952
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.801 Å)
Structure validation

217705

건을2024-03-27부터공개중

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