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- PDB-2hft: THE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN TISSUE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hft | |||||||||
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Title | THE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN TISSUE FACTOR AT 1.7 ANGSTROMS RESOLUTION | |||||||||
![]() | HUMAN TISSUE FACTOR | |||||||||
![]() | COAGULATION FACTOR | |||||||||
Function / homology | ![]() activation of blood coagulation via clotting cascade / activation of plasma proteins involved in acute inflammatory response / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / NGF-stimulated transcription / positive regulation of positive chemotaxis / Extrinsic Pathway of Fibrin Clot Formation / cytokine receptor activity / positive regulation of TOR signaling / positive regulation of endothelial cell proliferation ...activation of blood coagulation via clotting cascade / activation of plasma proteins involved in acute inflammatory response / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / NGF-stimulated transcription / positive regulation of positive chemotaxis / Extrinsic Pathway of Fibrin Clot Formation / cytokine receptor activity / positive regulation of TOR signaling / positive regulation of endothelial cell proliferation / positive regulation of interleukin-8 production / protein processing / phospholipid binding / cytokine-mediated signaling pathway / positive regulation of angiogenesis / activation of cysteine-type endopeptidase activity involved in apoptotic process / blood coagulation / collagen-containing extracellular matrix / protease binding / positive regulation of cell migration / external side of plasma membrane / positive regulation of gene expression / cell surface / extracellular space / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Muller, Y.A. / De Vos, A.M. | |||||||||
![]() | ![]() Title: The crystal structure of the extracellular domain of human tissue factor refined to 1.7 A resolution. Authors: Muller, Y.A. / Ultsch, M.H. / de Vos, A.M. #1: ![]() Title: Analysis of the Factor Viia Binding Site on Human Tissue Factor: Effects of Tissue Factor Mutations on the Kinetics and Thermodynamics of Binding Authors: Kelley, R.F. / Costas, K.E. / O'Connell, E.M. / Lazarus, R.A. #2: ![]() Title: Structure of the Extracellular Domain of Human Tissue Factor: Location of the Factor Viia Binding Site Authors: Muller, Y.A. / Ultsch, M.H. / Kelley, R.F. / De Vos, A.M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.8 KB | Display | ![]() |
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PDB format | ![]() | 43.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.5 KB | Display | ![]() |
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Full document | ![]() | 431.3 KB | Display | |
Data in XML | ![]() | 12.7 KB | Display | |
Data in CIF | ![]() | 18.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 27 |
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Components
#1: Protein | Mass: 24697.398 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
Compound details | THE FACTOR VII BINDING SITE WAS IDENTIFIED BY ALA-SCANNING MUTAGENESIS (KELLEY ET AL., 1995; SEE ...THE FACTOR VII BINDING SITE WAS IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.44 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | |||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 49 % | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 100 K / Method: vapor diffusion, sitting dropDetails: drop contains 0.05 ml of protein solution and 0.01 ml of reservoir solution | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Wavelength: 0.908 Å |
Detector | Type: FUJI FILM / Detector: IMAGE PLATE |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.908 Å / Relative weight: 1 |
Reflection | Resolution: 1.69→6 Å / Num. obs: 24199 / % possible obs: 97 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.058 |
Reflection | *PLUS Rmerge(I) obs: 0.058 |
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Processing
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Refinement | Resolution: 1.69→6 Å / σ(F): 0
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Displacement parameters | Biso mean: 27.6 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.69→6 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ/X-PLOR / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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