4YNP

ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM)

Summary for 4YNP

Entry DOI	10.2210/pdb4ynp/pdb
Related	4YNM
Descriptor	Histone-lysine N-methyltransferase ASH1L, ZINC ION, S-ADENOSYLMETHIONINE (3 entities in total)
Functional Keywords	histone methylation, set domain, transferase
Biological source	Homo sapiens (Human)
Total number of polymer chains	2
Total formula weight	53310.59
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: 26292256 DOI: 10.1021/acs.biochem.5b00697 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.9 Å)

Structure validation