1PEG

Structural basis for the product specificity of histone lysine methyltransferases

Summary for 1PEG

• Entry DOI: 10.2210/pdb1peg/pdb
• Related: 1ML9
• Descriptor: histone H3 methyltransferase DIM-5, Histone H3, ZINC ION, ... (4 entities in total)
• Functional Keywords: ternary structure of dim-5, a suv39-type histone-h3 lys-9 methyltransferase, set domain protein forms a knot-like substructure, pre-set triangular zn3cys9 zinc cluster, post-set zinc-binding site, a hybrid beta sheet formed by dim-5 and h3 tail, transferase
• Biological source: Neurospora crassa; More
• Cellular location: Nucleus (By similarity): Q8X225; Nucleus: P02303
• Total number of polymer chains: 4
• Total formula weight: 72646.79

Authors

Zhang, X.,Yang, Z.,Khan, S.I.,Horton, J.R.,Tamaru, H.,Selker, E.U.,Cheng, X. (deposition date: 2003-05-21, release date: 2003-08-05, Last modification date: 2023-08-16)

• Primary citation: Zhang, X.,Yang, Z.,Khan, S.I.,Horton, J.R.,Tamaru, H.,Selker, E.U.,Cheng, X.; Structural basis for the product specificity of histone lysine methyltransferases; Mol.Cell, 12:177-185, 2003; PubMed: 12887903; DOI: 10.1016/S1097-2765(03)00224-7

Experimental method

X-RAY DIFFRACTION (2.59 Å)