+Open data
-Basic information
Entry | Database: PDB / ID: 1fnj | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88S/R90K | ||||||
Components | PROTEIN (CHORISMATE MUTASE) | ||||||
Keywords | ISOMERASE / chorismate mutase / protein / mutant / pseudo-alpha beta-barrel / trimer | ||||||
Function / homology | Function and homology information chorismate metabolic process / chorismate mutase / chorismate mutase activity / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMEN / Resolution: 1.9 Å | ||||||
Authors | Kast, P. / Grisostomi, C. / Chen, I.A. / Li, S. / Krengel, U. / Xue, Y. / Hilvert, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000 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: Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 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: Journal: J.Am.Chem.Soc. / Year: 1999 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1fnj.cif.gz | 37.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1fnj.ent.gz | 24.6 KB | Display | PDB format |
PDBx/mmJSON format | 1fnj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fn/1fnj ftp://data.pdbj.org/pub/pdb/validation_reports/fn/1fnj | HTTPS FTP |
---|
-Related structure data
Related structure data | 1fnkC 2chtS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 14479.837 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) 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: Escherichia coli (E. coli) / References: UniProt: P19080, chorismate mutase |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 45 % | |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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
|
-Data collection
Diffraction | Mean temperature: 295 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Nov 1, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→30 Å / Num. obs: 10748 / % possible obs: 97.7 % / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Rsym value: 0.06 / Net I/σ(I): 29 |
Reflection shell | Resolution: 1.75→1.81 Å / Redundancy: 2.5 % / Rsym value: 0.068 / % possible all: 82.1 |
Reflection | *PLUS Highest resolution: 1.75 Å / Lowest resolution: 30 Å / Rmerge(I) obs: 0.06 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMEN Starting model: PDB# 2CHT Resolution: 1.9→30 Å / Cross valid method: R-FREE / σ(F): 2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→30 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.9→1.99 Å / Total num. of bins used: 8
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file | Serial no: 1 / Param file: PARHCSDX.PRO / Topol file: TOPHCSDX.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 30 Å / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.343 / % reflection Rfree: 3.4 % / Rfactor Rwork: 0.316 |