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- PDB-3btf: THE CRYSTAL STRUCTURES OF THE COMPLEXES BETWEEN BOVINE BETA-TRYPS... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3btf | ||||||
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Title | THE CRYSTAL STRUCTURES OF THE COMPLEXES BETWEEN BOVINE BETA-TRYPSIN AND TEN P1 VARIANTS OF BPTI. | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / TRYPSIN / BPTI / SERINE PROTEINASE / INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / trypsin / serpin family protein binding ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / protease binding / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Helland, R. / Otlewski, J. / Sundheim, O. / Dadlez, M. / Smalas, A.O. | ||||||
![]() | ![]() Title: The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI. Authors: Helland, R. / Otlewski, J. / Sundheim, O. / Dadlez, M. / Smalas, A.O. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 69.7 KB | Display | ![]() |
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PDB format | ![]() | 49.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426 KB | Display | ![]() |
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Full document | ![]() | 427.3 KB | Display | |
Data in XML | ![]() | 13.5 KB | Display | |
Data in CIF | ![]() | 18.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3btdC ![]() 3bteC ![]() 3btgC ![]() 3bthC ![]() 3btkC ![]() 3btmC ![]() 3btqC ![]() 3bttC ![]() 3btwC ![]() 2ptcS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||
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#2: Protein | Mass: 6527.524 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
#3: Chemical | ChemComp-CA / | ||||
#4: Chemical | ChemComp-SO4 / #5: Water | ChemComp-HOH / | Compound details | P1 RESIDUE OF THE INHIBITOR IS MUTATED TO PHE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.32 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: 0.1 M HEPES PH 7.5 48% AMMONIUM SULPHATE | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 37 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→15 Å / Num. obs: 36655 / % possible obs: 98.1 % / Redundancy: 4 % / Biso Wilson estimate: 20 Å2 / Rmerge(I) obs: 0.059 / Rsym value: 0.059 / Net I/σ(I): 8.4 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 4 % / Rmerge(I) obs: 0.326 / Mean I/σ(I) obs: 2.2 / Rsym value: 0.326 / % possible all: 98.8 |
Reflection shell | *PLUS % possible obs: 98.8 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2PTC Resolution: 1.8→8 Å / Cross valid method: THROUGHOUT / σ(F): 1 Details: ENERGY TERMS OF THE INHIBITOR SCISSILE PEPTIDE BOND WERE SET TO ZERO DURING REFINEMENT
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Displacement parameters | Biso mean: 21.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.9 Å / Total num. of bins used: 8 /
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Xplor file |
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