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- PDB-6at2: E. coli phosphoenolpyruvate carboxykinase G209N mutant bound to t... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6at2 | |||||||||
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Title | E. coli phosphoenolpyruvate carboxykinase G209N mutant bound to thiosulfate | |||||||||
![]() | Phosphoenolpyruvate carboxykinase (ATP) | |||||||||
![]() | LYASE / Nonnative ligand | |||||||||
Function / homology | ![]() phosphoenolpyruvate carboxykinase (ATP) / phosphoenolpyruvate carboxykinase (ATP) activity / gluconeogenesis / calcium ion binding / magnesium ion binding / ATP binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Tang, H.Y.H. / Shin, D.S. / Tainer, J.A. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase. Authors: Tang, H.Y.H. / Shin, D.S. / Hura, G.L. / Yang, Y. / Hu, X. / Lightstone, F.C. / McGee, M.D. / Padgett, H.S. / Yannone, S.M. / Tainer, J.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 212.1 KB | Display | ![]() |
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PDB format | ![]() | 165.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 23 KB | Display | |
Data in CIF | ![]() | 34.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6asiC ![]() 6asmC ![]() 6asnC ![]() 6at3C ![]() 6at4C ![]() 2olqS 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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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 60595.121 Da / Num. of mol.: 1 / Mutation: G209N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: pckA, pck, b3403, JW3366 / Production host: ![]() ![]() References: UniProt: P22259, phosphoenolpyruvate carboxykinase (ATP) |
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-Non-polymers , 6 types, 347 molecules ![](data/chem/img/ATP.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/THJ.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/THJ.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ATP / |
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#3: Chemical | ChemComp-MN / |
#4: Chemical | ChemComp-MG / |
#5: Chemical | ChemComp-TRS / |
#6: Chemical | ChemComp-THJ / |
#7: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.45 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 24% PEG 3350, 0.4 M sodium chloride, 0.1 M Bis-Tris pH 5.5, 0.1 M sodium thiosulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 6, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1158 Å / Relative weight: 1 |
Reflection | Resolution: 1.444→47.18 Å / Num. obs: 182988 / % possible obs: 96.3 % / Redundancy: 3.8 % / CC1/2: 0.995 / Rmerge(I) obs: 0.118 / Net I/σ(I): 7.48 |
Reflection shell | Resolution: 1.444→1.52 Å / Redundancy: 3.8 % / Rmerge(I) obs: 1.371 / Mean I/σ(I) obs: 1.04 / Num. unique obs: 28555 / CC1/2: 0.53 / % possible all: 92.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2OLQ Resolution: 1.444→47.18 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 21.89
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.444→47.18 Å
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Refine LS restraints |
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LS refinement shell |
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