+Open data
-Basic information
Entry | Database: PDB / ID: 2qft | ||||||
---|---|---|---|---|---|---|---|
Title | E.coli EPSP synthase Pro101Ser liganded with S3P and glyphosate | ||||||
Components | 3-phosphoshikimate 1-carboxyvinyltransferaseEPSP synthase | ||||||
Keywords | TRANSFERASE / inside-out alpha-beta barrel | ||||||
Function / homology | Function and homology information 3-phosphoshikimate 1-carboxyvinyltransferase / 3-phosphoshikimate 1-carboxyvinyltransferase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||
Authors | Schonbrunn, E. / Healy-Fried, M.L. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2007 Title: Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase. Authors: Healy-Fried, M.L. / Funke, T. / Priestman, M.A. / Han, H. / Schonbrunn, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2qft.cif.gz | 113.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2qft.ent.gz | 84.4 KB | Display | PDB format |
PDBx/mmJSON format | 2qft.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qf/2qft ftp://data.pdbj.org/pub/pdb/validation_reports/qf/2qft | HTTPS FTP |
---|
-Related structure data
Related structure data | 2qfqC 2qfsC 2qfuC 1g6sS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 46131.574 Da / Num. of mol.: 1 / Mutation: P101S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: aroA / Plasmid: pET24d / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P0A6D3, 3-phosphoshikimate 1-carboxyvinyltransferase | ||
---|---|---|---|
#2: Chemical | ChemComp-GPJ / | ||
#3: Chemical | ChemComp-S3P / | ||
#4: Chemical | ChemComp-FMT / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.9 % |
---|---|
Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Na-formate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Feb 12, 2007 / Details: osmic mirrors |
Radiation | Monochromator: osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→20 Å / Num. all: 63948 / Num. obs: 63948 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.02 / Net I/σ(I): 44.3 |
Reflection shell | Resolution: 1.55→1.6 Å / Rmerge(I) obs: 0.048 / Mean I/σ(I) obs: 20.6 / Num. unique all: 5744 / % possible all: 99.9 |
-Processing
Software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1G6S Resolution: 1.55→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): -3 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||
Solvent computation | Bsol: 61.561 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.461 Å2
| ||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.16 Å / Luzzati sigma a free: 0.07 Å | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→20 Å
| ||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||
Xplor file |
|