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- PDB-2ra3: Human cationic trypsin complexed with bovine pancreatic trypsin i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ra3 | ||||||
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Title | Human cationic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI) | ||||||
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![]() | hydrolase/hydrolase inhibitor / Human cationic trypsin / Serine protease / Bovine pancreatic trypsin inhibitor / BPTI / Calcium / Digestion / Disease mutation / Hydrolase / Metal-binding / Secreted / Sulfation / Zymogen / Pharmaceutical / Protease inhibitor / Serine protease inhibitor / hydrolase-hydrolase inhibitor COMPLEX | ||||||
Function / homology | ![]() Uptake of dietary cobalamins into enterocytes / trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / Activation of Matrix Metalloproteinases ...Uptake of dietary cobalamins into enterocytes / trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / Activation of Matrix Metalloproteinases / extracellular matrix disassembly / trypsin / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / protease binding / collagen-containing extracellular matrix / blood microparticle / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Salameh, M.A. / Soares, A.S. / Radisky, E.S. | ||||||
![]() | ![]() Title: Structural Basis for Accelerated Cleavage of Bovine Pancreatic Trypsin Inhibitor (BPTI) by Human Mesotrypsin. Authors: Salameh, M.A. / Soares, A.S. / Hockla, A. / Radisky, E.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 249.4 KB | Display | ![]() |
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PDB format | ![]() | 201.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2r9pC ![]() 1trnS ![]() 2ptcS C: citing same article ( 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 24102.154 Da / Num. of mol.: 2 / Mutation: R117H, S195A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 6527.568 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Chemical | #4: Chemical | ChemComp-SO4 / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.13 Å3/Da / Density % sol: 60.71 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.1M Tris hydrochloride pH 8.5, 1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 27, 2006 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Resolution: 1.46→26.144 Å / Num. obs: 115118 / % possible obs: 87.1 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 7.5 % / Biso Wilson estimate: 17.335 Å2 / Rmerge(I) obs: 0.057 / Rsym value: 0.057 / Net I/σ(I): 19.5 |
Reflection shell | Resolution: 1.46→1.54 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.465 / Mean I/σ(I) obs: 1.9 / Rsym value: 0.465 / % possible all: 46.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entries 1TRN and 2PTC Resolution: 1.46→26.13 Å / Isotropic thermal model: anisotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 16.36 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.46→26.13 Å
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Refine LS restraints |
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