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5F5E

The Crystal Structure of MLL1 SET domain with N3816I/Q3867L mutation

Summary for 5F5E
Entry DOI10.2210/pdb5f5e/pdb
Related5F59 5F6K 5F6L
DescriptorHistone-lysine N-methyltransferase 2A, ZINC ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
Functional Keywordshistone methyltransferase, histone methylation, set domain, transferase
Biological sourceHomo sapiens (Human)
Cellular locationNucleus . MLL cleavage product N320: Nucleus. MLL cleavage product C180: Nucleus: Q03164
Total number of polymer chains1
Total formula weight18693.01
Authors
Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-04, release date: 2016-02-24, Last modification date: 2023-11-08)
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 (1.802 Å)
Structure validation

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