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Open data
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Basic information
Entry | Database: PDB / ID: 2qfs | ||||||
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Title | E.coli EPSP synthase Pro101Ser liganded with S3P | ||||||
![]() | 3-phosphoshikimate 1-carboxyvinyltransferase | ||||||
![]() | TRANSFERASE / inside-out alpha-beta barrel | ||||||
Function / homology | ![]() 3-phosphoshikimate 1-carboxyvinyltransferase / 3-phosphoshikimate 1-carboxyvinyltransferase activity / shikimate kinase activity / shikimate 3-dehydrogenase (NADP+) activity / 3-dehydroquinate dehydratase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Schonbrunn, E. / Healy-Fried, M.L. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 111.1 KB | Display | ![]() |
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PDB format | ![]() | 82.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 797.6 KB | Display | ![]() |
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Full document | ![]() | 797.6 KB | Display | |
Data in XML | ![]() | 23 KB | Display | |
Data in CIF | ![]() | 36.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2qfqC ![]() 2qftC ![]() 2qfuC ![]() 1g6sS S: Starting model for refinement C: citing same article ( |
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Similar 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: 46131.574 Da / Num. of mol.: 1 / Mutation: P101S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() 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: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.71 % |
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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 |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Feb 20, 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: 63104 / Num. obs: 63104 / % possible obs: 98.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.025 / Net I/σ(I): 38.4 |
Reflection shell | Resolution: 1.55→1.6 Å / Rmerge(I) obs: 0.065 / Mean I/σ(I) obs: 14.7 / Num. unique all: 5588 / % possible all: 97.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1G6S Resolution: 1.55→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): -3 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 64.546 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.841 Å2
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Refine analyze | Luzzati coordinate error free: 0.16 Å / Luzzati sigma a free: 0.13 Å | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→20 Å
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Refine LS restraints |
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Xplor file |
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