The crystal structure of MLL3 SET domain

Summary for 5F59

Related5F5E 5F6L 5F6K
DescriptorHistone-lysine N-methyltransferase 2C, ZINC ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
Functional Keywordshistone methylation, histone methyltransferase, set domain, transferase
Biological sourceHomo sapiens (Human)
Cellular locationNucleus  Q8NEZ4
Total number of polymer chains1
Total molecular weight18453.42
Li, Y.,Lei, M.,Chen, Y. (deposition date: 2015-12-04, 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

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.2313002.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution