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基本情報
登録情報 | データベース: PDB / ID: 1i57 | ||||||
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タイトル | CRYSTAL STRUCTURE OF APO HUMAN PTP1B (C215S) MUTANT | ||||||
![]() | PHOSPHO-TYROSINE PHOSPHATASE 1B | ||||||
![]() | HYDROLASE / Substrate-trapping mutant / conformational change / WPD loop / phosphate-binding loop | ||||||
機能・相同性 | ![]() regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane ...regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane / platelet-derived growth factor receptor-beta signaling pathway / sorting endosome / mitochondrial crista / positive regulation of IRE1-mediated unfolded protein response / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / non-membrane spanning protein tyrosine phosphatase activity / positive regulation of protein tyrosine kinase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / regulation of signal transduction / cellular response to unfolded protein / growth hormone receptor signaling pathway via JAK-STAT / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of signal transduction / Regulation of IFNG signaling / Growth hormone receptor signaling / MECP2 regulates neuronal receptors and channels / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / Insulin receptor recycling / negative regulation of insulin receptor signaling pathway / ephrin receptor binding / Integrin signaling / protein dephosphorylation / protein-tyrosine-phosphatase / negative regulation of MAP kinase activity / protein phosphatase 2A binding / protein tyrosine phosphatase activity / endosome lumen / insulin receptor binding / Negative regulation of MET activity / negative regulation of ERK1 and ERK2 cascade / receptor tyrosine kinase binding / insulin receptor signaling pathway / actin cytoskeleton organization / early endosome / mitochondrial matrix / cadherin binding / protein kinase binding / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / zinc ion binding / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() ![]() ![]() | ||||||
![]() | Scapin, G. / Patel, S. / Patel, V. / Kennedy, B. / Asante-Appiah, E. | ||||||
![]() | ![]() タイトル: The structure of apo protein-tyrosine phosphatase 1B C215S mutant: more than just an S --> O change. 著者: Scapin, G. / Patel, S. / Patel, V. / Kennedy, B. / Asante-Appiah, E. #1: ![]() タイトル: The Single Sulfur to Oxygen Substitution in the Active Site Nucleofile of the Yersinia Protein-tyrosine Phosphatase Leads to Substantial Structural and Functional Perturbations 著者: Zhang, Z.Y. / Wu, L. #2: ![]() タイトル: Rapid Loop Dynamics of Yersinia Protein-Tyrosine Phosphatase 著者: Juszczak, L.J. / Zhang, Z.Y. / Wu, L. / Gottfried, D.S. / Eads, D.D. #3: ![]() タイトル: Conformational and Dynamic Changes of Yersinia Protein Tyrosine Phosphatase Induced by Ligand Binding and Active Site Mutation and Revealed by H/D Exchange and Electrospray Ionization ...タイトル: Conformational and Dynamic Changes of Yersinia Protein Tyrosine Phosphatase Induced by Ligand Binding and Active Site Mutation and Revealed by H/D Exchange and Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry 著者: Wang, F. / Li, W. / Emmett, M.R. / Hendrickson, C.L. / Marshall, A.G. / Zhang, Y.L. / Wu, L. / Zhang, Z.Y. #4: ![]() タイトル: Thermodynamic Study of Ligand Binding to Protein-tyrosine Phosphatase 1B and its Substrate-trapping Mutants. 著者: Zhang, Y.L. / Yao, Z.J. / Sarmiento, M. / Wu, L. / Burke, T.R. / Zhang, Z.Y. | ||||||
履歴 |
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Remark 999 | SEQUENCE THE FIRST 12 RESIDUES ARE THE KODAK FLAG USED FOR PURIFICATION. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 79.5 KB | 表示 | ![]() |
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PDB形式 | ![]() | 57.5 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 416.9 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 420.7 KB | 表示 | |
XML形式データ | ![]() | 15.3 KB | 表示 | |
CIF形式データ | ![]() | 22.3 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 | ![]() 1ptyS S: 精密化の開始モデル |
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類似構造データ |
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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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要素
#1: タンパク質 | 分子量: 36222.109 Da / 分子数: 1 / 断片: CATALYTIC DOMAIN (1-298) / 変異: C215S / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() | ||
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#2: 化合物 | ChemComp-MG / | ||
#3: 化合物 | ChemComp-CL / #4: 水 | ChemComp-HOH / | |
-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: 2.92 Å3/Da / 溶媒含有率: 57.85 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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結晶化 | 温度: 284 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 7 詳細: PEG 3350, Hepes, Magnesium Chloride, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 284K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
結晶 | *PLUS 溶媒含有率: 65 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
結晶化 | *PLUS 温度: 4 ℃ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
回折 | 平均測定温度: 100 K |
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放射光源 | 由来: ![]() ![]() ![]() |
検出器 | タイプ: MARRESEARCH / 検出器: CCD / 日付: 2000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 Å / 相対比: 1 |
反射 | 解像度: 2.1→20 Å / Num. all: 25206 / Num. obs: 25181 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / 冗長度: 10.3 % / Biso Wilson estimate: 42 Å2 / Rmerge(I) obs: 0.061 / Rsym value: 0.097 / Net I/σ(I): 11.7 |
反射 シェル | 解像度: 2.1→2.23 Å / 冗長度: 10.5 % / Rmerge(I) obs: 0.398 / Mean I/σ(I) obs: 1.9 / Num. unique all: 4136 / Rsym value: 0.0486 / % possible all: 100 |
反射 | *PLUS Num. measured all: 259144 |
反射 シェル | *PLUS % possible obs: 100 % / Num. unique obs: 4136 / Num. measured obs: 43394 |
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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: PDB ENTRY 1PTY 解像度: 2.1→20 Å / Isotropic thermal model: Restrained / 交差検証法: THROUGHOUT / σ(F): 0 / 立体化学のターゲット値: Engh & Huber 詳細: MD:Torsion annealing, constant, starting T=2000 Anisotropic B-correction resolution 6-2.1 Ang. Bulk solvent (mask) density level 0.360 e/A^3, B-factor = 58.95 A^2
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溶媒の処理 | 溶媒モデル: mask / Bsol: 59 Å2 / ksol: 0.36 e/Å3 | |||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 40.3 Å2
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精密化ステップ | サイクル: LAST / 解像度: 2.1→20 Å
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拘束条件 |
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LS精密化 シェル | 解像度: 2.1→2.2 Å
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ソフトウェア | *PLUS 名称: CNS / 分類: refinement | |||||||||||||||||||||||||
精密化 | *PLUS 最高解像度: 2.1 Å / 最低解像度: 20 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor all: 0.21 / Rfactor obs: 0.195 | |||||||||||||||||||||||||
溶媒の処理 | *PLUS | |||||||||||||||||||||||||
原子変位パラメータ | *PLUS Biso mean: 40.3 Å2 | |||||||||||||||||||||||||
LS精密化 シェル | *PLUS Rfactor Rfree: 0.432 / Rfactor Rwork: 0.309 |