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5F6K

Crystal structure of the MLL3-Ash2L-RbBP5 complex

Summary for 5F6K
Entry DOI10.2210/pdb5f6k/pdb
Related5F59 5F5E 5F5L
DescriptorSet1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2, Histone-lysine N-methyltransferase 2C, Retinoblastoma-binding protein 5, ... (7 entities in total)
Functional Keywordshistone methylation, histone methyltransferase, mll-family proteins, set domain, transferase-protein binding complex, transferase/protein binding
Biological sourceHomo sapiens (Human)
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Cellular locationNucleus : Q9UBL3 Q8NEZ4 Q15291
Total number of polymer chains7
Total formula weight86552.41
Authors
Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-06, 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 (2.411 Å)
Structure validation

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