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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: 1ai8 | ||||||
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タイトル | HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH THE EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROMPG | ||||||
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![]() | BLOOD COAGULATION/HYDROLASE INHIBITOR / SERINE PROTEINASE / BLOOD COAGULATION / HYDROLASE-HYDROLASE INHIBITOR COMPLEX / BLOOD COAGULATION-HYDROLASE INHIBITOR complex | ||||||
機能・相同性 | ![]() negative regulation of serine-type peptidase activity / positive regulation of lipid kinase activity / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / cytolysis by host of symbiont cells / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / ligand-gated ion channel signaling pathway ...negative regulation of serine-type peptidase activity / positive regulation of lipid kinase activity / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / cytolysis by host of symbiont cells / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / ligand-gated ion channel signaling pathway / Defective F8 cleavage by thrombin / Platelet Aggregation (Plug Formation) / negative regulation of astrocyte differentiation / negative regulation of platelet activation / positive regulation of collagen biosynthetic process / negative regulation of cytokine production involved in inflammatory response / positive regulation of blood coagulation / negative regulation of fibrinolysis / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / regulation of cytosolic calcium ion concentration / fibrinolysis / Intrinsic Pathway of Fibrin Clot Formation / Peptide ligand-binding receptors / positive regulation of release of sequestered calcium ion into cytosol / acute-phase response / Regulation of Complement cascade / negative regulation of proteolysis / Cell surface interactions at the vascular wall / lipopolysaccharide binding / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / serine-type endopeptidase inhibitor activity / positive regulation of insulin secretion / platelet activation / response to wounding / positive regulation of protein localization to nucleus / Golgi lumen / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of reactive oxygen species metabolic process / antimicrobial humoral immune response mediated by antimicrobial peptide / blood coagulation / Thrombin signalling through proteinase activated receptors (PARs) / heparin binding / regulation of cell shape / positive regulation of cell growth / G alpha (q) signalling events / collagen-containing extracellular matrix / blood microparticle / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / serine-type endopeptidase activity / signaling receptor binding / calcium ion binding / positive regulation of cell population proliferation / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | ![]() ![]() | ||||||
![]() | Skordalakes, E. / Dodson, G. / Elgendy, S. / Goodwin, C.A. / Green, D. / Tyrrel, R. / Scully, M.F. / Freyssinet, J. / Kakkar, V.V. / Deadman, J. | ||||||
![]() | ![]() タイトル: The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed ...タイトル: The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. 著者: Bode, W. / Turk, D. / Karshikov, A. #1: ![]() タイトル: The Refined 1.9 A Crystal Structure of Human Alpha-Thrombin: Interaction with D-Phe-Pro-Arg Chloromethylketone and Significance of the Tyr-Pro-Pro-Trp Insertion Segment 著者: Bode, W. / Mayr, I. / Baumann, U. / Huber, R. / Stone, S.R. / Hofsteenge, J. | ||||||
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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PDBx/mmCIF形式 | ![]() | 78.2 KB | 表示 | ![]() |
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PDB形式 | ![]() | 60.3 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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要素
#1: タンパク質・ペプチド | 分子量: 4096.534 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
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#2: タンパク質 | 分子量: 29780.219 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
#3: タンパク質・ペプチド | 分子量: 1606.616 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
#4: 化合物 | ChemComp-T42 / |
#5: 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: 2.48 Å3/Da / 溶媒含有率: 45 % | |||||||||||||||
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結晶化 | 温度: 277 K / pH: 7.2 詳細: PROTEIN COMPLEX WAS CRYSTALLIZED FROM 25% PEG 8000 0.05 SODIUM PHOSPHATE, PH 7.2, TEMPERATURE 277 K. | |||||||||||||||
結晶化 | *PLUS pH: 7 / 手法: microdialysis / 詳細: Bode, W., (1989) EMBO J., 8, 3467. | |||||||||||||||
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: RIGAKU RAXIS II / 検出器: IMAGE PLATE / 日付: 1996年11月15日 / 詳細: MIRRORS |
放射 | モノクロメーター: NI FILTER / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 1.5418 Å / 相対比: 1 |
反射 | 解像度: 1.85→20 Å / Num. obs: 29239 / % possible obs: 96.1 % / Observed criterion σ(I): 0 / 冗長度: 2.6 % / Rmerge(I) obs: 0.0645 / Rsym value: 0.048 / Net I/σ(I): 13 |
反射 シェル | 解像度: 1.85→1.9 Å / 冗長度: 2 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 2 / Rsym value: 0.38 / % possible all: 92.5 |
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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 1DWE 解像度: 1.85→20 Å / σ(F): 0 詳細: THE CLOSE CONTACTS FOR RESIDUES H 91 - H 196, H 147 - H 146, AND I 60 - I 59 ARE DUE TO THE DIFFICULTY OF REFINING THESE RESIDUES. THESE RESIDUES ARE NOT WELL DEFINED IN THE ELECTRON DENSITY MAP.
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精密化ステップ | サイクル: LAST / 解像度: 1.85→20 Å
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ソフトウェア | *PLUS 名称: REFMAC / 分類: refinement | ||||||||||||||||
精密化 | *PLUS Rfactor all: 0.17 | ||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||
原子変位パラメータ | *PLUS |