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Open data
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Basic information
Entry | Database: PDB / ID: 1fnk | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88K/R90S | ||||||
![]() | PROTEIN (CHORISMATE MUTASE) | ||||||
![]() | ISOMERASE / CHORISMATE MUTASE / PROTEIN / MUTANT / PSEUDO-ALPHA BETA-BARREL / TRIMER | ||||||
Function / homology | ![]() chorismate metabolic process / chorismate mutase / chorismate mutase activity / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kast, P. / Grisostomi, C. / Chen, I.A. / Li, S. / Krengel, U. / Xue, Y. / Hilvert, D. | ||||||
![]() | ![]() Title: A strategically positioned cation is crucial for efficient catalysis by chorismate mutase. Authors: Kast, P. / Grisostomi, C. / Chen, I.A. / Li, S. / Krengel, U. / Xue, Y. / Hilvert, D. #1: ![]() Title: Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis Authors: Kast, P. / Asif-Ullah, M. / Jiang, N. / Hilvert, D. #2: ![]() Title: Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase Authors: Gustin, D.J. / Mattei, P. / Kast, P. / Wiest, O. / Lee, L. / Cleland, W.W. / Hilvert, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 32.3 KB | Display | ![]() |
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PDB format | ![]() | 24.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.8 KB | Display | ![]() |
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Full document | ![]() | 426.3 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Data in CIF | ![]() | 8.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 14495.835 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid details: PET-22B(+) FROM NOVAGEN (MADISON, WI) AND PKET3-W, A PET-22B(+) DERIVATIVE ALLOWING FOR T7 PROMOTOR-DRIVEN GENE EXPRESSION Plasmid: PET-22B(+), PKET3-W / Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.51 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Protein solution: 10 mM Tris-HCl, 2mM DTT, 0.125 mM EDTA, Reservoir solution: 30% PEG 400, 50 mM Tris-HCl, 50 mM magnesium chloride, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS PH range low: 7.5 / PH range high: 7 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→30 Å / Num. obs: 9357 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Rmerge(I) obs: 0.085 |
Reflection | *PLUS Highest resolution: 1.85 Å / Lowest resolution: 30 Å |
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Processing
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Refinement | Resolution: 2→30 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 30 Å | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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