4YNM
ASH1L wild-type SET domain in complex with S-adenosyl methionine (SAM)
Summary for 4YNM
Entry DOI | 10.2210/pdb4ynm/pdb |
Related | 4YNP |
Descriptor | Histone-lysine N-methyltransferase ASH1L, ZINC ION, S-ADENOSYLMETHIONINE, ... (4 entities in total) |
Functional Keywords | histone methylation, set domain, transferase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 53222.36 |
Authors | Rogawski, D.S.,Ndoj, J.,Cho, H.-J.,Maillard, I.,Grembecka, J.,Cierpicki, T. (deposition date: 2015-03-10, release date: 2015-09-02, Last modification date: 2023-09-27) |
Primary citation | Rogawski, D.S.,Ndoj, J.,Cho, H.J.,Maillard, I.,Grembecka, J.,Cierpicki, T. Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase. Biochemistry, 54:5401-5413, 2015 Cited by PubMed: 26292256DOI: 10.1021/acs.biochem.5b00697 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
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