3UVM
Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4
Summary for 3UVM
Entry DOI | 10.2210/pdb3uvm/pdb |
Related | 3UVK 3UVL 3UVN 3UVO |
Descriptor | WD repeat-containing protein 5, Histone-lysine N-methyltransferase MLL4 (3 entities in total) |
Functional Keywords | trithorax, chromatin biology, beta-propeller, scaffolding, histone h3, nucleus, transcription |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus: P61964 Nucleus (By similarity): Q9UMN6 |
Total number of polymer chains | 2 |
Total formula weight | 35901.71 |
Authors | Zhang, P.,Lee, H.,Brunzelle, J.S.,Couture, J.-F. (deposition date: 2011-11-30, release date: 2011-12-14, Last modification date: 2023-09-13) |
Primary citation | Zhang, P.,Lee, H.,Brunzelle, J.S.,Couture, J.F. The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases. Nucleic Acids Res., 40:4237-4246, 2012 Cited by PubMed: 22266653DOI: 10.1093/nar/gkr1235 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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