2A0T
NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1
2A0T の概要
| エントリーDOI | 10.2210/pdb2a0t/pdb |
| 分子名称 | Serine/threonine-protein kinase RAD53, Hypothetical 73.8 kDa protein in SAS3-SEC17 intergenic region, residues 301-310 (2 entities in total) |
| 機能のキーワード | fha domain. rad53, mdt1, phosphothreonine, phosphoprotein, transferase |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) 詳細 |
| 細胞内の位置 | Nucleus: P22216 Cytoplasm: P34217 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 18339.66 |
| 構造登録者 | Mahajan, A.,Yuan, C.,Pike, B.L.,Heierhorst, J.,Chang, C.-F.,Tsai, M.-D. (登録日: 2005-06-16, 公開日: 2005-11-08, 最終更新日: 2024-11-13) |
| 主引用文献 | Mahajan, A.,Yuan, C.,Pike, B.L.,Heierhorst, J.,Chang, C.-F.,Tsai, M.-D. FHA Domain-Ligand Interactions: Importance of Integrating Chemical and Biological Approaches J.Am.Chem.Soc., 127:14572-14573, 2005 Cited by PubMed Abstract: Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions. PubMed: 16231900DOI: 10.1021/ja054538m 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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