5F5E
The Crystal Structure of MLL1 SET domain with N3816I/Q3867L mutation
Summary for 5F5E
Entry DOI | 10.2210/pdb5f5e/pdb |
Related | 5F59 5F6K 5F6L |
Descriptor | Histone-lysine N-methyltransferase 2A, ZINC ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total) |
Functional Keywords | histone methyltransferase, histone methylation, set domain, transferase |
Biological source | Homo sapiens (Human) |
Cellular location | Nucleus . MLL cleavage product N320: Nucleus. MLL cleavage product C180: Nucleus: Q03164 |
Total number of polymer chains | 1 |
Total formula weight | 18693.01 |
Authors | |
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 Cited by PubMed: 26886794DOI: 10.1038/nature16952 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.802 Å) |
Structure validation
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