+Open data
-Basic information
Entry | Database: PDB / ID: 2qfq | ||||||
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Title | E. coli EPSP synthase Pro101Leu liganded with S3P | ||||||
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: 1.5 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qfq.cif.gz | 109.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qfq.ent.gz | 81.2 KB | Display | PDB format |
PDBx/mmJSON format | 2qfq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qf/2qfq ftp://data.pdbj.org/pub/pdb/validation_reports/qf/2qfq | HTTPS FTP |
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-Related structure data
Related structure data | 2qfsC 2qftC 2qfuC 1g6sS S: Starting model for refinement C: citing same article (ref.) |
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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: 46157.656 Da / Num. of mol.: 1 / Mutation: P101L 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 | ||
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#2: Chemical | ChemComp-S3P / | ||
#3: Chemical | ChemComp-FMT / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.35 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Na-formate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: May 3, 2005 / 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: 1.5→20 Å / Num. all: 69786 / Num. obs: 69786 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.048 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 1.5→1.55 Å / Rmerge(I) obs: 0.171 / Mean I/σ(I) obs: 6.6 / Num. unique all: 6428 / % possible all: 99.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1g6s Resolution: 1.5→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): -3 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 43.562 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.066 Å2
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Refine analyze | Luzzati coordinate error free: 0.16 Å / Luzzati sigma a free: 0.11 Å | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→20 Å
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Refine LS restraints |
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Xplor file |
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