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; PubMed: 26292256; DOI: 10.1021/acs.biochem.5b00697

Experimental method

X-RAY DIFFRACTION (2.19 Å)