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- PDB-3vv2: Crystal structure of complex form between S324A-subtilisin and mu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3vv2 | ||||||
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Title | Crystal structure of complex form between S324A-subtilisin and mutant Tkpro | ||||||
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![]() | HYDROLASE / Proteolysis | ||||||
Function / homology | ![]() Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type endopeptidase activity / proteolysis / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Uehara, R. / Ueda, Y. / You, D.J. / Takano, K. / Koga, Y. / Kanaya, S. | ||||||
![]() | ![]() Title: Accelerated maturation of Tk-subtilisin by a Leu Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisin Authors: Uehara, R. / Ueda, Y. / You, D.J. / Koga, Y. / Kanaya, 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 | ![]() | 89.4 KB | Display | ![]() |
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PDB format | ![]() | 65.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2z30S 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
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 33897.562 Da / Num. of mol.: 1 / Fragment: UNP residues 94-422 / Mutation: S324A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P58502, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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#2: Protein | Mass: 7496.786 Da / Num. of mol.: 1 / Fragment: UNP residues 25-93 / Mutation: L69P Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 118 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-CA / #4: Chemical | ChemComp-CL / | #5: Chemical | ChemComp-ZN / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.36 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.1M Sodium cacodylate, 0.2M Zinc acetate, 2% PEG4000, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 2, 2011 |
Radiation | Monochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.83→50 Å / Num. obs: 28926 / % possible obs: 96.7 % / Observed criterion σ(F): 5 / Observed criterion σ(I): 5 |
Reflection shell | Resolution: 1.83→1.86 Å / % possible all: 93.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2Z30 Resolution: 1.83→31.12 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.896 / SU B: 3.768 / SU ML: 0.115 / Cross valid method: THROUGHOUT / ESU R: 0.18 / ESU R Free: 0.166 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.1 Å2
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Refinement step | Cycle: LAST / Resolution: 1.83→31.12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.83→1.878 Å / Total num. of bins used: 20
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