+Open data
-Basic information
Entry | Database: PDB / ID: 2gga | ||||||
---|---|---|---|---|---|---|---|
Title | CP4 EPSP synthase liganded with S3P and Glyphosate | ||||||
Components | 3-phosphoshikimate 1-carboxyvinyltransferaseEPSP synthase | ||||||
Keywords | TRANSFERASE / inside-out alpha/beta barrel / two domain structure | ||||||
Function / homology | Function and homology information 3-phosphoshikimate 1-carboxyvinyltransferase / 3-phosphoshikimate 1-carboxyvinyltransferase activity / response to herbicide / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | Agrobacterium sp. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Schonbrunn, E. / Funke, T. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2006 Title: Molecular basis for the herbicide resistance of Roundup Ready crops. Authors: Funke, T. / Han, H. / Healy-Fried, M.L. / Fischer, M. / Schonbrunn, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2gga.cif.gz | 107.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2gga.ent.gz | 80.1 KB | Display | PDB format |
PDBx/mmJSON format | 2gga.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gg/2gga ftp://data.pdbj.org/pub/pdb/validation_reports/gg/2gga | HTTPS FTP |
---|
-Related structure data
Related structure data | 2gg4C 2gg6SC 2ggdC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 47637.340 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Agrobacterium sp. (bacteria) / Strain: CP4 / Gene: aroA / Plasmid: pET21a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: Q9R4E4, 3-phosphoshikimate 1-carboxyvinyltransferase |
---|---|
#2: Chemical | ChemComp-S3P / |
#3: Chemical | ChemComp-GPJ / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.23 % |
---|---|
Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: (NH4)2SO4 / KCl / PEG 400 / HEPES-Na , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 90 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 17, 2005 / Details: mirrors |
Radiation | Monochromator: rigaku mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→15 Å / Num. all: 45806 / Num. obs: 44653 / % possible obs: 99.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.07 / Net I/σ(I): 29.3 |
Reflection shell | Resolution: 1.7→1.74 Å / Rmerge(I) obs: 0.377 / Mean I/σ(I) obs: 4.6 / Num. unique all: 2965 / % possible all: 97.3 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2GG6 Resolution: 1.7→15 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): -3 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→15 Å
| |||||||||||||||||||||||||
Refine LS restraints |
|