5F59

The crystal structure of MLL3 SET domain

Summary for 5F59

• Entry DOI: 10.2210/pdb5f59/pdb
• Related: 5F5E 5F6K 5F6L
• Descriptor: Histone-lysine N-methyltransferase 2C, ZINC ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• Functional Keywords: histone methylation, histone methyltransferase, set domain, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : Q8NEZ4
• Total number of polymer chains: 1
• Total formula weight: 18453.42

Authors

Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-04, release date: 2016-02-24, Last modification date: 2024-03-20)

• Primary citation: Li, 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; PubMed: 26886794; DOI: 10.1038/nature16952

Experimental method

X-RAY DIFFRACTION (2.801 Å)