5M7R
Structure of human O-GlcNAc hydrolase
5M7R の概要
エントリーDOI | 10.2210/pdb5m7r/pdb |
分子名称 | Protein O-GlcNAcase (2 entities in total) |
機能のキーワード | human glacoside hydrolase glcnac, hydrolase |
由来する生物種 | Homo sapiens (Human) |
細胞内の位置 | Isoform 3: Nucleus . Isoform 1: Cytoplasm : O60502 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 206041.81 |
構造登録者 | Roth, C.,Chan, S.,Offen, W.A.,Hemsworth, G.R.,Willems, L.I.,King, D.,Varghese, V.,Britton, R.,Vocadlo, D.J.,Davies, G.J. (登録日: 2016-10-28, 公開日: 2017-03-29, 最終更新日: 2024-01-17) |
主引用文献 | Roth, C.,Chan, S.,Offen, W.A.,Hemsworth, G.R.,Willems, L.I.,King, D.T.,Varghese, V.,Britton, R.,Vocadlo, D.J.,Davies, G.J. Structural and functional insight into human O-GlcNAcase. Nat. Chem. Biol., 13:610-612, 2017 Cited by PubMed Abstract: O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value. PubMed: 28346405DOI: 10.1038/nchembio.2358 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.35 Å) |
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