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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DOI10.2210/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: 16231900
DOI: 10.1021/ja054538m
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2a0t
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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