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- PDB-7cts: Open form of PET-degrading cutinase Cut190 with thermostability-i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7cts | ||||||
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Title | Open form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation | ||||||
![]() | Alpha/beta hydrolase family protein | ||||||
![]() | HYDROLASE / PROTEIN ENGINEERING / POLYESTERASE / disulfide bond / metal binding | ||||||
Function / homology | Platelet-activating factor acetylhydrolase, isoform II / cutinase / carboxylic ester hydrolase activity / Alpha/Beta hydrolase fold / metal ion binding / 1,4-DIETHYLENE DIOXIDE / cutinase![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Emori, M. / Numoto, N. / Senga, A. / Bekker, G.J. / Kamiya, N. / Ito, N. / Kawai, F. / Oda, M. | ||||||
![]() | ![]() Title: Structural basis of mutants of PET-degrading enzyme from Saccharomonospora viridis AHK190 with high activity and thermal stability. Authors: Emori, M. / Numoto, N. / Senga, A. / Bekker, G.J. / Kamiya, N. / Kobayashi, Y. / Ito, N. / Kawai, F. / Oda, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.1 KB | Display | ![]() |
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PDB format | ![]() | 102.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.6 KB | Display | ![]() |
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Full document | ![]() | 446.7 KB | Display | |
Data in XML | ![]() | 16.1 KB | Display | |
Data in CIF | ![]() | 25.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7ctrC ![]() 4wfjS S: Starting model for refinement C: citing same article ( |
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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: 28889.537 Da / Num. of mol.: 1 Mutation: S226P, R228S, Q138A, D250C, E296C, Q123H, N202H, S176A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-DIO / |
#3: Chemical | ChemComp-BCN / |
#4: Chemical | ChemComp-CA / |
#5: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.48 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.1M Bicine, 2% (v/v) 1,4-dioxane, 10% (w/v) PEG 20000 |
-Data collection
Diffraction | Mean temperature: 95 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 1, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→31 Å / Num. obs: 125717 / % possible obs: 96 % / Redundancy: 5.8 % / Biso Wilson estimate: 11.32 Å2 / CC1/2: 0.999 / Rsym value: 0.06 / Net I/σ(I): 13.4 |
Reflection shell | Resolution: 1.1→1.16 Å / Mean I/σ(I) obs: 1.1 / Num. unique obs: 19227 / CC1/2: 0.599 / Rsym value: 1.06 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4WFJ Resolution: 1.1→30.02 Å / SU ML: 0.1294 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 16.7348 / Stereochemistry target values: GeoStd + Monomer Library
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.92 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→30.02 Å
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Refine LS restraints |
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LS refinement shell |
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