5F5E

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

Summary for 5F5E

Related5F59 5F6L 5F6K
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 molecular weight18693.02
Authors
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
X-RAY DIFFRACTION (1.802 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.236700.8%8.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report