4HC4

Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae)

Summary for 4HC4

• Entry DOI: 10.2210/pdb4hc4/pdb
• Descriptor: Protein arginine N-methyltransferase 6, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: hrmt1l6, methyltransferase, s-adenosyl-l-homocysteine, structural genomics, structural genomics consortium, sgc, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q96LA8
• Total number of polymer chains: 1
• Total formula weight: 42613.13

Authors

Dong, A.,Zeng, H.,He, H.,El Bakkouri, M.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Brown, P.J.,Wu, H.,Structural Genomics Consortium (SGC) (deposition date: 2012-09-28, release date: 2012-10-17, Last modification date: 2023-09-20)

• Primary citation: Wu, H.,Zheng, W.,Eram, M.S.,Vhuiyan, M.,Dong, A.,Zeng, H.,He, H.,Brown, P.,Frankel, A.,Vedadi, M.,Luo, M.,Min, J.; Structural basis of arginine asymmetrical dimethylation by PRMT6.; Biochem. J., 473:3049-3063, 2016; PubMed: 27480107; DOI: 10.1042/BCJ20160537

Experimental method

X-RAY DIFFRACTION (1.97 Å)