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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 6y40 | ||||||
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タイトル | 14-3-3 Sigma in complex with phosphorylated PLN peptide | ||||||
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![]() | PROTEIN BINDING / 14-3-3 / PLN / complex / protein / protein-protein interactions | ||||||
機能・相同性 | ![]() phospholamban complex / regulation of ATPase-coupled calcium transmembrane transporter activity / negative regulation of calcium ion binding / circadian sleep/wake cycle, sleep / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / negative regulation of calcium ion import into sarcoplasmic reticulum / regulation of relaxation of cardiac muscle / negative regulation of ATPase-coupled calcium transmembrane transporter activity / regulation of the force of heart contraction by cardiac conduction / calcium ion-transporting ATPase complex ...phospholamban complex / regulation of ATPase-coupled calcium transmembrane transporter activity / negative regulation of calcium ion binding / circadian sleep/wake cycle, sleep / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / negative regulation of calcium ion import into sarcoplasmic reticulum / regulation of relaxation of cardiac muscle / negative regulation of ATPase-coupled calcium transmembrane transporter activity / regulation of the force of heart contraction by cardiac conduction / calcium ion-transporting ATPase complex / regulation of cardiac muscle cell membrane potential / acrosome assembly / negative regulation of calcium ion transmembrane transporter activity / negative regulation of catalytic activity / negative regulation of calcium ion import / regulation of the force of heart contraction / negative regulation of ATP-dependent activity / ATPase inhibitor activity / regulation of cardiac muscle cell contraction / cardiac muscle tissue development / blood circulation / relaxation of cardiac muscle / negative regulation of heart rate / muscle cell cellular homeostasis / regulation of epidermal cell division / protein kinase C inhibitor activity / regulation of heart contraction / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / locomotor rhythm / regulation of cell-cell adhesion / Ion transport by P-type ATPases / negative regulation of calcium ion transport / enzyme inhibitor activity / cAMP/PKA signal transduction / regulation of calcium ion transport / Regulation of localization of FOXO transcription factors / keratinocyte proliferation / phosphoserine residue binding / Activation of BAD and translocation to mitochondria / negative regulation of keratinocyte proliferation / regulation of cytosolic calcium ion concentration / establishment of skin barrier / negative regulation of protein localization to plasma membrane / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / negative regulation of stem cell proliferation / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / Ion homeostasis / RHO GTPases activate PKNs / positive regulation of protein localization / Notch signaling pathway / sarcoplasmic reticulum membrane / positive regulation of cell adhesion / protein sequestering activity / negative regulation of innate immune response / protein export from nucleus / release of cytochrome c from mitochondria / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / sarcoplasmic reticulum / positive regulation of protein export from nucleus / negative regulation of protein kinase activity / stem cell proliferation / Translocation of SLC2A4 (GLUT4) to the plasma membrane / TP53 Regulates Metabolic Genes / mitochondrial membrane / visual learning / intracellular calcium ion homeostasis / intrinsic apoptotic signaling pathway in response to DNA damage / intracellular protein localization / regulation of protein localization / ATPase binding / positive regulation of cell growth / regulation of cell cycle / cadherin binding / endoplasmic reticulum membrane / protein kinase binding / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / signal transduction / protein homodimerization activity / mitochondrion / extracellular space / extracellular exosome / identical protein binding / nucleus / membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() ![]() | ||||||
![]() | Ballone, A. / Lau, R.A. / Zweipfenning, F.P.A. / Ottmann, C. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes. 著者: Ballone, A. / Lau, R.A. / Zweipfenning, F.P.A. / Ottmann, C. | ||||||
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 | ![]() | 94.3 KB | 表示 | ![]() |
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PDB形式 | ![]() | 55.9 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-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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単位格子 |
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Components on special symmetry positions |
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要素
#1: タンパク質・ペプチド | 分子量: 1948.166 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() | ||||||||
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#2: タンパク質 | 分子量: 28226.518 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() | ||||||||
#3: 化合物 | #4: 化合物 | ChemComp-CL / | #5: 水 | ChemComp-HOH / | 研究の焦点であるリガンドがあるか | Y | Has protein modification | Y | |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.4 Å3/Da / 溶媒含有率: 48.7 % |
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結晶化 | 温度: 277 K / 手法: 蒸気拡散法, ハンギングドロップ法 詳細: PEG400, 1.25% glycerol, 0.2M CaCl, 0.1M HEPES pH 7.5, 2mM BME |
-データ収集
回折 | 平均測定温度: 100 K / Serial crystal experiment: N |
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放射光源 | 由来: SEALED TUBE / タイプ: RIGAKU / 波長: 1.541 Å |
検出器 | タイプ: DECTRIS PILATUS 200K / 検出器: PIXEL / 日付: 2019年10月16日 |
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 1.541 Å / 相対比: 1 |
反射 | 解像度: 1.59→41.81 Å / Num. obs: 31591 / % possible obs: 80.2 % / Biso Wilson estimate: 9.62 Å2 / CC1/2: 0.996 / Net I/σ(I): 14.3 |
反射 シェル | 解像度: 1.59→1.63 Å / Num. unique obs: 31591 / CC1/2: 0.937 / % possible all: 98.8 |
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解析
ソフトウェア |
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精密化 | 構造決定の手法: ![]() 開始モデル: 3LW1 解像度: 1.75→41.81 Å / SU ML: 0.1565 / 交差検証法: FREE R-VALUE / σ(F): 1.34 / 位相誤差: 19.4398
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溶媒の処理 | 減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 12.59 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 解像度: 1.75→41.81 Å
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拘束条件 |
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LS精密化 シェル |
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