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基本情報
登録情報 | データベース: PDB / ID: 1nmw | ||||||
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タイトル | Solution structure of the PPIase domain of human Pin1 | ||||||
![]() | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | ||||||
![]() | ISOMERASE / PPIase domain / beta-alpha / a1/b1 loop / sulphate | ||||||
機能・相同性 | ![]() cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / regulation of protein localization to nucleus / GTPase activating protein binding / postsynaptic cytosol / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division / negative regulation of SMAD protein signal transduction ...cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / regulation of protein localization to nucleus / GTPase activating protein binding / postsynaptic cytosol / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division / negative regulation of SMAD protein signal transduction / PI5P Regulates TP53 Acetylation / negative regulation of amyloid-beta formation / cytoskeletal motor activity / phosphoserine residue binding / RHO GTPases Activate NADPH Oxidases / protein peptidyl-prolyl isomerization / positive regulation of protein dephosphorylation / ciliary basal body / positive regulation of GTPase activity / regulation of cytokinesis / negative regulation of protein binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / Negative regulators of DDX58/IFIH1 signaling / phosphoprotein binding / synapse organization / negative regulation of transforming growth factor beta receptor signaling pathway / regulation of protein phosphorylation / regulation of protein stability / tau protein binding / neuron differentiation / negative regulation of protein catabolic process / negative regulation of ERK1 and ERK2 cascade / ISG15 antiviral mechanism / beta-catenin binding / positive regulation of canonical Wnt signaling pathway / positive regulation of protein binding / midbody / regulation of gene expression / Regulation of TP53 Activity through Phosphorylation / protein stabilization / response to hypoxia / nuclear speck / positive regulation of protein phosphorylation / cell cycle / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR / torsion angle dynamics | ||||||
![]() | Bayer, E. / Goettsch, S. / Mueller, J.W. / Griewel, B. / Guiberman, E. / Mayr, L. / Bayer, P. | ||||||
![]() | ![]() タイトル: Structural Analysis of the Mitotic Regulator hPin1 in Solution: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE BINDING. 著者: Bayer, E. / Goettsch, S. / Mueller, J.W. / Griewel, B. / Guiberman, E. / Mayr, L.M. / Bayer, P. #1: ![]() タイトル: A human peptidyl-prolyl isomerase essential for regulation of mitosis 著者: Lu, K.P. / Hannes, S.D. / Hunter, T. #2: ![]() タイトル: Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent 著者: Ranganathan, R. / Lu, K.P. / Hunter, T. / Noel, J.P. #3: ![]() タイトル: Structural basis for phosphoserine-proline recognition by group IV WW domains 著者: Verdecia, M.A. / Bowman, M.E. / Lu, K.P. / Hunter, T. / Noel, J.P. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDB形式 | ![]() | 292.8 KB | 表示 | ![]() |
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その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 364.3 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 451 KB | 表示 | |
XML形式データ | ![]() | 23.2 KB | 表示 | |
CIF形式データ | ![]() | 36.4 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 1nmvC C: 同じ文献を引用 ( |
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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: 12765.312 Da / 分子数: 1 / 断片: PPIase domain (residues 50-163) / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
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#2: 化合物 | ChemComp-SO4 / |
-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: Hydrogen bonds were extracted from HSQC spectra in D2O |
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試料調製
詳細 |
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試料状態 |
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結晶化 | *PLUS 手法: other / 詳細: NMR |
-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: Varian INOVA / 製造業者: Varian / モデル: INOVA / 磁場強度: 600 MHz |
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解析
NMR software |
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精密化 | 手法: torsion angle dynamics / ソフトェア番号: 1 | ||||||||||||||||||||||||
代表構造 | 選択基準: lowest energy | ||||||||||||||||||||||||
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: 100 / 登録したコンフォーマーの数: 10 |