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- PDB-1sfi: High resolution structure of a potent, cyclic protease inhibitor ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1sfi | ||||||
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Title | High resolution structure of a potent, cyclic protease inhibitor from sunflower seeds | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / TRYPSIN INHIBITOR / CYCLIC PEPTIDE / PROTEASE / BOVINE-TRYPSIN / SERINE PROTEASE-INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() negative regulation of endopeptidase activity / endopeptidase inhibitor activity / trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / protease binding / serine-type endopeptidase activity ...negative regulation of endopeptidase activity / endopeptidase inhibitor activity / trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / protease binding / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Luckett, S. / Garcia, R.S. / Barker, J.J. / Konarev, A.V. / Shewry, P. / Clarke, A.R. / Brady, R.L. | ||||||
![]() | ![]() Title: High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. Authors: Luckett, S. / Garcia, R.S. / Barker, J.J. / Konarev, A.V. / Shewry, P.R. / Clarke, A.R. / Brady, R.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 62.7 KB | Display | ![]() |
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PDB format | ![]() | 47.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 376.6 KB | Display | ![]() |
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Full document | ![]() | 376.8 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 11.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1tldS 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: 23324.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||
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#2: Protein/peptide | ![]() ![]() ![]() | ||||||
#3: Chemical | #4: Chemical | ChemComp-CA / | #5: Water | ChemComp-HOH / | Compound details | CYCLIC PEPTIDE BOUND TO ACTIVE SITE OF TRYPSIN NO 3'-TERMINAL RESIDUE, CYCLIC PEPTIDE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 54.8 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: IMAGE PLATE / Date: May 1, 1998 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.448 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→20 Å / Num. obs: 32839 / % possible obs: 96.7 % / Redundancy: 2.5 % / Biso Wilson estimate: 18.43 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 14 |
Reflection shell | Resolution: 1.65→1.78 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.223 / Mean I/σ(I) obs: 3.8 / % possible all: 91 |
Reflection | *PLUS Num. measured all: 82087 |
Reflection shell | *PLUS % possible obs: 91 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1TLD Resolution: 1.65→20 Å / SU B: 1.67 / SU ML: 0.06 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.09 / ESU R Free: 0.09
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Displacement parameters | Biso mean: 21.11 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.203 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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