2L3R
NMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide
Summary for 2L3R
Entry DOI | 10.2210/pdb2l3r/pdb |
NMR Information | BMRB: 17200 |
Descriptor | E3 ubiquitin-protein ligase UHRF1, Histone H3 (2 entities in total) |
Functional Keywords | tudor domain, heterochromatin, transcriptional repression, structural genomics, structural genomics consortium, sgc, dna binding protein, dna binding protein-gene regulation complex, dna binding protein/gene regulation |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 20174.53 |
Authors | Nady, N.,Lemak, A.,Fares, C.,Gutmanas, A.,Avvakumov, G.,Xue, S.,Arrowsmith, C.,Structural Genomics Consortium (SGC) (deposition date: 2010-09-21, release date: 2011-04-13, Last modification date: 2020-02-05) |
Primary citation | Nady, N.,Lemak, A.,Walker, J.R.,Avvakumov, G.V.,Kareta, M.S.,Achour, M.,Xue, S.,Duan, S.,Allali-Hassani, A.,Zuo, X.,Wang, Y.X.,Bronner, C.,Chedin, F.,Arrowsmith, C.H.,Dhe-Paganon, S. Recognition of Multivalent Histone States Associated with Heterochromatin by UHRF1 Protein. J.Biol.Chem., 286:24300-24311, 2011 Cited by PubMed: 21489993DOI: 10.1074/jbc.M111.234104 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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