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- PDB-8grj: Crystal structure of gamma-alpha subunit complex from Burkholderi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8grj | ||||||
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Title | Crystal structure of gamma-alpha subunit complex from Burkholderia cepacia FAD glucose dehydrogenase in complex with gluconolactone | ||||||
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![]() | OXIDOREDUCTASE / Glucose dehydrogenase / FAD / Burkholderia cepacia / SIGNALING PROTEIN-OXIDOREDUCTASE complex | ||||||
Function / homology | ![]() oxidoreductase activity, acting on CH-OH group of donors / 3 iron, 4 sulfur cluster binding / flavin adenine dinucleotide binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yoshida, H. / Kojima, K. / Tsugawa, W. / Okuda-Shimazaki, J. / Kerrigan, J.A. / Sode, K. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Crystal structure of gamma-alpha subunit complex from Burkholderia cepacia FAD glucose dehydrogenase in complex with gluconolactone Authors: Yoshida, H. / Kojima, K. / Tsugawa, W. / Okuda-Shimazaki, J. / Kerrigan, J.A. / Sode, K. #1: ![]() Title: X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein. Authors: Yoshida, H. / Kojima, K. / Shiota, M. / Yoshimatsu, K. / Yamazaki, T. / Ferri, S. / Tsugawa, W. / Kamitori, S. / Sode, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 267.8 KB | Display | ![]() |
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PDB format | ![]() | 214 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 49.9 KB | Display | |
Data in CIF | ![]() | 68.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6a2uS S: Starting model for refinement |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 2 types, 4 molecules ACBD
#1: Protein | Mass: 17980.414 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: GB:CAZ78686.1 / Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 60735.762 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: GB:AAN39686.1 / Source: (gene. exp.) ![]() ![]() ![]() |
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-Sugars , 1 types, 2 molecules ![](data/chem/img/LGC.gif)
#5: Sugar |
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-Non-polymers , 3 types, 153 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/F3S.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/F3S.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.86 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: Tacsimate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 13, 2013 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.95→100 Å / Num. obs: 42134 / % possible obs: 99.4 % / Redundancy: 15.5 % / Rmerge(I) obs: 0.113 / Χ2: 0.955 / Net I/σ(I): 7.4 / Num. measured all: 653811 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6A2U Resolution: 2.95→50.04 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.846 / SU B: 16.465 / SU ML: 0.298 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.412 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 117.89 Å2 / Biso mean: 37.59 Å2 / Biso min: 0.5 Å2
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Refinement step | Cycle: final / Resolution: 2.95→50.04 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.95→3.022 Å / Rfactor Rfree error: 0
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