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基本情報
登録情報 | データベース: PDB / ID: 1k3n | ||||||
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タイトル | NMR Structure of the FHA1 Domain of Rad53 in Complex with a Rad9-derived Phosphothreonine (at T155) Peptide | ||||||
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![]() | TRANSFERASE/CELL CYCLE / FHA domain / Rad53 / rad9 / phosphothreonine / phosphoprotein / TRANSFERASE-CELL CYCLE COMPLEX | ||||||
機能・相同性 | ![]() deoxyribonucleoside triphosphate biosynthetic process / negative regulation of DNA strand resection involved in replication fork processing / meiotic recombination checkpoint signaling / telomere maintenance in response to DNA damage / SUMOylation of transcription factors / negative regulation of phosphorylation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / dual-specificity kinase / mitotic intra-S DNA damage checkpoint signaling / DNA replication origin binding ...deoxyribonucleoside triphosphate biosynthetic process / negative regulation of DNA strand resection involved in replication fork processing / meiotic recombination checkpoint signaling / telomere maintenance in response to DNA damage / SUMOylation of transcription factors / negative regulation of phosphorylation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / dual-specificity kinase / mitotic intra-S DNA damage checkpoint signaling / DNA replication origin binding / negative regulation of DNA damage checkpoint / DNA replication initiation / regulation of DNA repair / enzyme activator activity / mitotic G1 DNA damage checkpoint signaling / protein serine/threonine/tyrosine kinase activity / DNA damage checkpoint signaling / nucleotide-excision repair / protein localization / double-strand break repair / histone binding / double-stranded DNA binding / protein tyrosine kinase activity / regulation of cell cycle / protein kinase activity / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / chromatin / positive regulation of transcription by RNA polymerase II / ATP binding / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | 溶液NMR / The complex structures are generated using a total of 2438 restraints. Among them, 3 artifical constraints, 192 TALOS-derived dihedral angle restrains, 78 restraints from H-bond, 16 intermolecular distance constrains, and 2149 intra-FHA1, intra-peptide distance constraints. | ||||||
![]() | Yuan, C. / Yongkiettrakul, S. / Byeon, I.-J.L. / Zhou, S. / Tsai, M.-D. | ||||||
![]() | ![]() タイトル: Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. 著者: Yuan, C. / Yongkiettrakul, S. / Byeon, I.J. / Zhou, S. / Tsai, M.D. #1: ![]() タイトル: Structure of the FHA1 Domain of Yeast Rad53 and Identification of Binding Sites for Both FHA1 and Its Target Protein Rad9. 著者: Liao, H. / Yuan, C. / Su, M.I. / Yongkiettrakul, S. / Qin, D. / Li, H. / Byeon, I.J. / Pei, D. / Tsai, M.D. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 1 MB | 表示 | ![]() |
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PDB形式 | ![]() | 898.9 KB | 表示 | ![]() |
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-検証レポート
文書・要旨 | ![]() | 363 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 614.5 KB | 表示 | |
XML形式データ | ![]() | 84.1 KB | 表示 | |
CIF形式データ | ![]() | 102.2 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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NMR アンサンブル |
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要素
#1: タンパク質 | 分子量: 17093.490 Da / 分子数: 1 / 断片: N-terminal FHA domain (FHA1) / 由来タイプ: 組換発現 由来: (組換発現) ![]() ![]() 遺伝子: SPK1 or Rad53 / プラスミド: pGEX-4T / 生物種 (発現宿主): Escherichia coli / 発現宿主: ![]() ![]() 参照: UniProt: P22216, 転移酵素; リンを含む基を移すもの; キナーゼ(アルコールにつなげるもの) |
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#2: タンパク質・ペプチド | 分子量: 1617.754 Da / 分子数: 1 / 断片: Residues 149-161 / 由来タイプ: 合成 詳細: This phosphothreonine peptide was chemically synthesized. 参照: UniProt: P14737 |
-実験情報
-実験
実験 | 手法: 溶液NMR | ||||||||||||||||||||
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NMR実験 |
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NMR実験の詳細 | Text: The structure was determined using triple-resonance NMR spectroscopy. |
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試料調製
詳細 | 内容: 0.5 mM FHA1 U-15N,13C; 10 mM sodium phosphate buffer (pH 6.5), 1mM DTT, and 1 mM EDTA; 90% H2O, 10% D2O 溶媒系: 90% H2O/10% D2O |
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試料状態 | イオン強度: 10 mM sodium phosphate, 1mM DTT, and 1 mM EDTA pH: 6.5 / 圧: ambient / 温度: 293 K |
-NMR測定
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M |
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放射波長 | 相対比: 1 |
NMRスペクトロメーター | タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 800 MHz |
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解析
NMR software |
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精密化 | 手法: The complex structures are generated using a total of 2438 restraints. Among them, 3 artifical constraints, 192 TALOS-derived dihedral angle restrains, 78 restraints from H-bond, 16 ...手法: The complex structures are generated using a total of 2438 restraints. Among them, 3 artifical constraints, 192 TALOS-derived dihedral angle restrains, 78 restraints from H-bond, 16 intermolecular distance constrains, and 2149 intra-FHA1, intra-peptide distance constraints. ソフトェア番号: 1 | ||||||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the least restraint violations,structures with the lowest energy 計算したコンフォーマーの数: 50 / 登録したコンフォーマーの数: 20 |