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Yorodumi- PDB-2ec9: Crystal structure analysis of human Factor VIIa , Souluble tissue... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ec9 | ||||||
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Title | Crystal structure analysis of human Factor VIIa , Souluble tissue factor complexed with BCX-3607 | ||||||
Components |
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Keywords | BLOOD CLOTTING / protein-cofactor complex / FVIIa and souluble tissue factor / inhibitor | ||||||
Function / homology | Function and homology information 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 | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Raman, K. / Yarlagadda, B. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2007 Title: Probing the S2 site of factor VIIa to generate potent and selective inhibitors: the structure of BCX-3607 in complex with tissue factor-factor VIIa. Authors: Krishnan, R. / Kotian, P.L. / Chand, P. / Bantia, S. / Rowland, S. / Babu, Y.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ec9.cif.gz | 140.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ec9.ent.gz | 107.2 KB | Display | PDB format |
PDBx/mmJSON format | 2ec9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ec9_validation.pdf.gz | 823.7 KB | Display | wwPDB validaton report |
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Full document | 2ec9_full_validation.pdf.gz | 857.6 KB | Display | |
Data in XML | 2ec9_validation.xml.gz | 31.3 KB | Display | |
Data in CIF | 2ec9_validation.cif.gz | 42.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ec/2ec9 ftp://data.pdbj.org/pub/pdb/validation_reports/ec/2ec9 | HTTPS FTP |
-Related structure data
Related structure data | 1danS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Coagulation factor ... , 2 types, 2 molecules LH
#1: Protein | Mass: 16359.772 Da / Num. of mol.: 1 / Fragment: residues 1-142 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): BHK / References: UniProt: P08709, coagulation factor VIIa |
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#2: Protein | Mass: 28103.256 Da / Num. of mol.: 1 / Fragment: residues 16-257 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): BHK / References: UniProt: P08709, coagulation factor VIIa |
-Protein , 2 types, 2 molecules TU
#3: Protein | Mass: 8715.800 Da / Num. of mol.: 1 / Fragment: residues 38-112 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): BHK / References: UniProt: P13726 |
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#4: Protein | Mass: 13745.301 Da / Num. of mol.: 1 / Fragment: residues 91-210 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): BHK / References: UniProt: P13726 |
-Sugars , 2 types, 2 molecules
#5: Sugar | ChemComp-ASO / |
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#6: Sugar | ChemComp-FUC / |
-Non-polymers , 3 types, 234 molecules
#7: Chemical | ChemComp-CA / #8: Chemical | ChemComp-24X / | #9: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 53.74 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 14% (w/v)PEG 4K, 0.1M MgCl2, 0.1M ADA buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 98 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Sep 12, 2004 / Details: osmic mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→25 Å / Num. all: 48960 / Num. obs: 47808 / % possible obs: 88 % / Observed criterion σ(F): 3 / Observed criterion σ(I): 1.5 / Redundancy: 4.2 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.357 / Mean I/σ(I) obs: 3.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1DAN Resolution: 2→25 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 3 / σ(I): 1.5 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 39 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→25 Å
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Refine LS restraints |
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