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- PDB-8fxt: Escherichia coli periplasmic Glucose-Binding Protein glucose comp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8fxt | ||||||
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Title | Escherichia coli periplasmic Glucose-Binding Protein glucose complex: Acrylodan conjugate attached at W183C | ||||||
![]() | D-galactose/methyl-galactoside binding periplasmic protein MglB | ||||||
![]() | SUGAR BINDING PROTEIN / Periplasmic binding protein / Biosensor Fluorescent conjugate | ||||||
Function / homology | ![]() carbohydrate transport / chemotaxis / outer membrane-bounded periplasmic space / carbohydrate binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Allert, M.J. / Kumar, S. / Wang, Y. / Beese, L.S. / Hellinga, H.W. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Chromophore carbonyl twisting in fluorescent biosensors encodes direct readout of protein conformations with multicolor switching. Authors: Allert, M.J. / Kumar, S. / Wang, Y. / Beese, L.S. / Hellinga, H.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.2 KB | Display | ![]() |
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PDB format | ![]() | 61.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 689.1 KB | Display | ![]() |
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Full document | ![]() | 689.2 KB | Display | |
Data in XML | ![]() | 16.4 KB | Display | |
Data in CIF | ![]() | 24.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8fxuC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
Experimental dataset #1 | Data reference: ![]() |
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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: 32864.027 Da / Num. of mol.: 1 / Mutation: W183C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Sugars , 2 types, 6 molecules ![](data/chem/img/GLC.gif)
![](data/chem/img/BGC.gif)
![](data/chem/img/BGC.gif)
#3: Sugar | ChemComp-GLC / |
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#4: Sugar | ChemComp-BGC / |
-Non-polymers , 3 types, 320 molecules ![](data/chem/img/YDM.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-YDM / |
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#5: Chemical | ChemComp-CA / |
#6: Water | ChemComp-HOH / |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.9 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / Details: 20% PEG 3350 0.2M potassium thiocyanate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 11, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.53→50 Å / Num. obs: 43030 / % possible obs: 98.8 % / Redundancy: 6.5 % / Biso Wilson estimate: 12.57 Å2 / Rmerge(I) obs: 0.06 / Rpim(I) all: 0.025 / Net I/σ(I): 25.54 |
Reflection shell | Resolution: 1.53→1.56 Å / Rmerge(I) obs: 0.292 / Mean I/σ(I) obs: 3.99 / Num. unique obs: 2019 / Rpim(I) all: 0.131 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.98 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.53→24.75 Å
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Refine LS restraints |
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LS refinement shell |
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