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- PDB-1pfg: Strategy to design inhibitors: Structure of a complex of Proteina... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pfg | ||||||
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Title | Strategy to design inhibitors: Structure of a complex of Proteinase K with a designed octapeptide inhibitor N-Ac-Pro-Ala-Pro-Phe-DAla-Ala-Ala-Ala-NH2 at 2.5A resolution | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / Proteinase K / octapeptide / inhibitor / complex / hydrolase / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() peptidase K / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Saxena, A.K. / Singh, T.P. / Peters, K. / Fittkau, S. / Betzel, C. | ||||||
![]() | ![]() Title: Strategy to design peptide inhibitors: structure of a complex of proteinase K with a designed octapeptide inhibitor N-Ac-Pro-Ala-Pro-Phe-DAla-Ala-Ala-Ala-NH2 at 2.5 A resolution. Authors: Saxena, A.K. / Singh, T.P. / Peters, K. / Fittkau, S. / Betzel, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 70.3 KB | Display | ![]() |
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PDB format | ![]() | 50.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 375.7 KB | Display | ![]() |
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Full document | ![]() | 405.4 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 17.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1pekS 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: 28958.838 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein/peptide | Mass: 738.853 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Solution phase synthesis |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43.6 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 50mM Tris, 1mM CaCl2, 1M NaHNO3, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 16 ℃ / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SEALED TUBE / Type: CONVENTIONAL Cu / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 3, 1995 / Details: Graphite monochromator |
Radiation | Monochromator: Graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. all: 49646 / Num. obs: 7647 / % possible obs: 83 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.065 / Rsym value: 0.069 |
Reflection | *PLUS Num. measured all: 49646 / Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1PEK Resolution: 2.5→8 Å / σ(F): 0 / σ(I): 0 Details: The distance between (B PHE 284) and Residue (B ALA 285) is longer than the peptide bond distance as the peptide is hydolysed at this point.
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Refine analyze | Luzzati coordinate error obs: 0.19 Å / Luzzati d res low obs: 8 Å / Luzzati sigma a obs: 0.17 Å | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||
Refine LS restraints | *PLUS
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