5F6L

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

Summary for 5F6L

Related5F5E 5F59 5F6K
DescriptorRetinoblastoma-binding protein 5, Set1/Ash2 histone methyltransferase complex subunit ASH2, Histone-lysine N-methyltransferase 2A, ... (6 entities in total)
Functional Keywordshistone methyltransferase, histone methylation, set domain, protein complex, protein binding-transferase complex, protein binding/transferase
Biological sourceHomo sapiens (Human)
Cellular locationNucleus  Q15291 Q9UBL3
Nucleus . MLL cleavage product N320: Nucleus. MLL cleavage product C180: Nucleus Q03164
Total number of polymer chains3
Total molecular weight42545.69
Authors
Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-06, release date: 2016-02-24, Last modification date: 2016-04-20)
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 (PDB entries with the same primary citation)
DOI: 10.1038/nature16952
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.9 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.214201.3%1.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution