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- PDB-1p2n: Structural consequences of accommodation of four non-cognate amin... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1p2n | ||||||
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Title | Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin | ||||||
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![]() | hydrolase/hydrolase inhibitor / trypsin / chymotrypsin / serine proteinase / bovine pancreatic trypsin inhibitor / protein-protein interaction / non-cognate binding / S1 pocket / primary specificity / crystal structure / hydrolase-hydrolase inhibitor COMPLEX | ||||||
Function / homology | ![]() chymotrypsin / 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 / serpin family protein binding ...chymotrypsin / 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 / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / protease binding / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Helland, R. / Czapinska, H. / Leiros, I. / Olufsen, M. / Otlewski, J. / Smalaas, A.O. | ||||||
![]() | ![]() Title: Structural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin. Authors: Helland, R. / Czapinska, H. / Leiros, I. / Olufsen, M. / Otlewski, J. / Smalaas, 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 | ![]() | 136 KB | Display | ![]() |
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PDB format | ![]() | 105.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 447.2 KB | Display | ![]() |
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Full document | ![]() | 449.2 KB | Display | |
Data in XML | ![]() | 28.4 KB | Display | |
Data in CIF | ![]() | 41.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1p2iC ![]() 1p2jC ![]() 1p2kC ![]() 1p2mC ![]() 1p2oC ![]() 1p2qC ![]() 1cbwS 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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Unit cell |
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Components
#1: Protein | Mass: 25686.037 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 6493.508 Da / Num. of mol.: 2 / Mutation: K15L, M52L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.21 Å3/Da / Density % sol: 70.56 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 50% ammonium sulfate, 0.1M Tris, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 19, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9312 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→24 Å / Num. all: 104176 / Num. obs: 104176 / % possible obs: 97.4 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Biso Wilson estimate: 21.96 Å2 / Rmerge(I) obs: 0.061 / Rsym value: 0.061 / Net I/σ(I): 5.7 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 2.4 / Num. unique all: 104221 / Rsym value: 0.18 / % possible all: 95.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1cbw Resolution: 1.8→24 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 24.02 Å2 | |||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å / Luzzati sigma a obs: 0.14 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→24 Å
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Refine LS restraints |
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