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- PDB-2zp0: Human factor viia-tissue factor complexed with benzylsulfonamide-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2zp0 | ||||||
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Title | Human factor viia-tissue factor complexed with benzylsulfonamide-D-ile-gln-P-aminobenzamidine | ||||||
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![]() | HYDROLASE/BLOOD CLOTTING / SERINE PROTEASE / Blood coagulation / Cleavage on pair of basic residues / Disease mutation / EGF-like domain / Gamma-carboxyglutamic acid / Glycoprotein / Hydrolase / Hydroxylation / Protease / Zymogen / Lipoprotein / Membrane / Palmitate / Transmembrane / HYDROLASE-BLOOD CLOTTING COMPLEX | ||||||
Function / homology | ![]() activation of blood coagulation via clotting cascade / activation of plasma proteins involved in acute inflammatory response / coagulation factor VIIa / response to Thyroid stimulating hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to astaxanthin / response to thyrotropin-releasing hormone / response to genistein / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway ...activation of blood coagulation via clotting cascade / activation of plasma proteins involved in acute inflammatory response / coagulation factor VIIa / response to Thyroid stimulating hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to astaxanthin / response to thyrotropin-releasing hormone / response to genistein / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / response to vitamin K / response to carbon dioxide / response to thyroxine / NGF-stimulated transcription / response to cholesterol / response to growth hormone / positive regulation of positive chemotaxis / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of leukocyte chemotaxis / cytokine receptor activity / positive regulation of TOR signaling / positive regulation of blood coagulation / animal organ regeneration / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Removal of aminoterminal propeptides from gamma-carboxylated proteins / positive regulation of endothelial cell proliferation / serine-type peptidase activity / BMAL1:CLOCK,NPAS2 activates circadian gene expression / positive regulation of interleukin-8 production / protein processing / phospholipid binding / cytokine-mediated signaling pathway / Golgi lumen / circadian rhythm / response to estrogen / positive regulation of angiogenesis / activation of cysteine-type endopeptidase activity involved in apoptotic process / blood coagulation / response to estradiol / collagen-containing extracellular matrix / protease binding / vesicle / response to hypoxia / positive regulation of cell migration / endoplasmic reticulum lumen / external side of plasma membrane / serine-type endopeptidase activity / signaling receptor binding / calcium ion binding / positive regulation of gene expression / cell surface / extracellular space / extracellular region / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kadono, S. / Sakamoto, A. / Kikuchi, Y. / Oh-eda, M. / Yabuta, N. / Koga, T. / Hattori, K. / Shiraishi, T. / Haramura, M. / Kodama, H. | ||||||
![]() | ![]() Title: Peptide Mimetic Factor VIIa Inhibitor: Importance of Hydrophilic Pocket in S2 Site to Improve Selectivity aganist Thrombin Authors: Kadono, S. / Sakamoto, A. / Kikuchi, Y. / Oh-eda, M. / Yabuta, N. / Koga, T. / Hattori, K. / Shiraishi, T. / Haramura, M. / Kodama, H. / Esaki, T. / Sato, H. / Watanabe, S. / Itoh, S. / Ohta, M. / Kozono, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 143.3 KB | Display | ![]() |
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PDB format | ![]() | 109.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 867.4 KB | Display | ![]() |
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Full document | ![]() | 885.5 KB | Display | |
Data in XML | ![]() | 28.9 KB | Display | |
Data in CIF | ![]() | 40.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1danS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 3 types, 3 molecules LHT
#1: Protein | Mass: 17487.076 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 28103.256 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein | Mass: 24697.398 Da / Num. of mol.: 1 / Fragment: RESIDUES 16-257 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Sugars , 2 types, 2 molecules ![](data/chem/img/BGC.gif)
![](data/chem/img/FUC.gif)
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#4: Sugar | ChemComp-BGC / |
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#5: Sugar | ChemComp-FUC / |
-Non-polymers , 3 types, 309 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/PI0.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PI0.gif)
![](data/chem/img/HOH.gif)
#6: Chemical | ChemComp-CA / #7: Chemical | ChemComp-PI0 / ( | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.07 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 8 % PEG 5000, 0.1M sodium chloride, 0.005M calcium chloride, 0.1M cacodylate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Feb 29, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→40 Å / Num. obs: 19950 / % possible obs: 96.5 % / Biso Wilson estimate: 30 Å2 / Rmerge(I) obs: 0.103 / Net I/σ(I): 4.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1DAN Resolution: 2.7→14.94 Å / Data cutoff high absF: 1882353.02 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 18.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→14.94 Å
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Refine LS restraints |
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Xplor file |
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