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Yorodumi- PDB-3kv8: Structural basis of the activity and substrate specificity of the... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3kv8 | ||||||
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Title | Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - Wild type FlK in complex with fluoro-acetate | ||||||
Components | Fluoroacetyl-CoA thioesterase FlK | ||||||
Keywords | HYDROLASE / fluoroacetyl-CoA thioesterase FlK / thioesterase / hot-dog folding | ||||||
Function / homology | Function and homology information fluoroacetyl-CoA thioesterase / acyl-CoA hydrolase activity / protein homodimerization activity Similarity search - Function | ||||||
Biological species | Streptomyces Cattleya (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.85 Å | ||||||
Authors | Dias, M.V.B. / Huang, F. / Chirgadze, D.Y. / Tosin, M. / Spiteller, D. / Valentine, E.F. / Leadlay, P.F. / Spencer, J.B. / Blundell, T.L. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2010 Title: Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK. Authors: Dias, M.V. / Huang, F. / Chirgadze, D.Y. / Tosin, M. / Spiteller, D. / Dry, E.F. / Leadlay, P.F. / Spencer, J.B. / Blundell, T.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3kv8.cif.gz | 70.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3kv8.ent.gz | 52.1 KB | Display | PDB format |
PDBx/mmJSON format | 3kv8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3kv8_validation.pdf.gz | 453.4 KB | Display | wwPDB validaton report |
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Full document | 3kv8_full_validation.pdf.gz | 457.6 KB | Display | |
Data in XML | 3kv8_validation.xml.gz | 15.9 KB | Display | |
Data in CIF | 3kv8_validation.cif.gz | 22.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kv/3kv8 ftp://data.pdbj.org/pub/pdb/validation_reports/kv/3kv8 | HTTPS FTP |
-Related structure data
Related structure data | 3kuvC 3kuwC 3kv7C 3kviC 3kvuC 3kvzC 3kw1C 3kx7C 3kx8C 1hnnS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 15279.436 Da / Num. of mol.: 2 / Fragment: FlK Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces Cattleya (bacteria) / Gene: flK, fluoroacetyl-CoA thioesterase FlK / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q1EMV2, Hydrolases #2: Chemical | ChemComp-FAH / #3: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.22 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Tris HCl PEG4000 Sodium Fluoroacetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: 2008 / Details: mirrors |
Radiation | Monochromator: single crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→30.59 Å / Num. all: 24031 / Num. obs: 23674 / % possible obs: 98.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 1.85→1.95 Å / % possible all: 98 |
-Processing
Software |
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Refinement | Starting model: PDB entry 1HNN Resolution: 1.85→28.67 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.928 / SU B: 2.825 / SU ML: 0.088 / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / ESU R: 0.134 / ESU R Free: 0.138 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.88 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→28.67 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.85→1.895 Å / Total num. of bins used: 20
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