1MT6
Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy
1MT6 の概要
| エントリーDOI | 10.2210/pdb1mt6/pdb |
| 関連するPDBエントリー | 1MUF |
| 分子名称 | SET9, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total) |
| 機能のキーワード | set domain, histone lysine methyltransferase, adohcy, knot, transferase |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Nucleus: Q8WTS6 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 31534.82 |
| 構造登録者 | Jacobs, S.A.,Harp, J.M.,Devarakonda, S.,Kim, Y.,Rastinejad, F.,Khorasanizadeh, S. (登録日: 2002-09-20, 公開日: 2002-11-06, 最終更新日: 2024-02-14) |
| 主引用文献 | Jacobs, S.A.,Harp, J.M.,Devarakonda, S.,Kim, Y.,Rastinejad, F.,Khorasanizadeh, S. The active site of the SET domain is constructed on a knot Nat.Struct.Biol., 9:833-838, 2002 Cited by PubMed Abstract: The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain. PubMed: 12389038主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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