5F6L

The crystal structure of MLL1 (N3861I/Q3867L) in complex with RbBP5 and Ash2L

Summary for 5F6L

Entry DOI	10.2210/pdb5f6l/pdb
Related	5F59 5F5E 5F6K
Descriptor	Retinoblastoma-binding protein 5, Set1/Ash2 histone methyltransferase complex subunit ASH2, Histone-lysine N-methyltransferase 2A, ... (6 entities in total)
Functional Keywords	histone methyltransferase, histone methylation, set domain, protein complex, protein binding-transferase complex, protein binding/transferase
Biological source	Homo sapiens (Human) More
Cellular location	Nucleus : Q15291 Q9UBL3 Nucleus . MLL cleavage product N320: Nucleus. MLL cleavage product C180: Nucleus: Q03164
Total number of polymer chains	3
Total formula weight	42545.69
Authors	Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-06, release date: 2016-02-24, Last modification date: 2023-11-08)
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: 26886794 DOI: 10.1038/nature16952 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation