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- PDB-5x7r: Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltra... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5x7r | |||||||||
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Title | Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose | |||||||||
![]() | Glycoside hydrolase family 31 alpha-glucosidase | |||||||||
![]() | HYDROLASE / TRANSFERASE / glydoside hydrolase family 31 / carbohydrate-binding module family 35 / carbohydrate-binding module family 61 | |||||||||
Function / homology | ![]() hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / carbohydrate metabolic process / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Fujimoto, Z. / Kishine, N. / Suzuki, N. / Momma, M. / Ichinose, H. / Kimura, A. / Funane, K. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Carbohydrate-binding architecture of the multi-modular alpha-1,6-glucosyltransferase from Paenibacillus sp. 598K, which produces alpha-1,6-glucosyl-alpha-glucosaccharides from starch Authors: Fujimoto, Z. / Suzuki, N. / Kishine, N. / Ichinose, H. / Momma, M. / Kimura, A. / Funane, K. #1: Journal: Appl. Microbiol. Biotechnol. / Year: 2017 Title: Paenibacillus sp. 598K 6-alpha-glucosyltransferase is essential for cycloisomaltooligosaccharide synthesis from alpha-(1 -> 4)-glucan Authors: Ichinose, H. / Suzuki, R. / Miyazaki, T. / Kimura, K. / Momma, M. / Suzuki, N. / Fujimoto, Z. / Kimura, A. / Funane, 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 | ![]() | 549.1 KB | Display | ![]() |
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PDB format | ![]() | 434.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.8 MB | Display | ![]() |
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Full document | ![]() | 2.8 MB | Display | |
Data in XML | ![]() | 99.8 KB | Display | |
Data in CIF | ![]() | 150.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5x7oSC ![]() 5x7pC ![]() 5x7qC ![]() 5x7sC 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 on special symmetry positions |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 137684.219 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: A0A193PKW5, Transferases; Glycosyltransferases; Hexosyltransferases, alpha-glucosidase |
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-Sugars , 6 types, 11 molecules ![](data/chem/img/BGC.gif)
![](data/chem/img/GLC.gif)
![](data/chem/img/GLC.gif)
#2: Polysaccharide | alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D- ...alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||||||
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#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Polysaccharide | #5: Polysaccharide | #7: Sugar | #8: Sugar | |
-Non-polymers , 7 types, 1722 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/NI.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NI.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
#6: Chemical | ChemComp-CA / #9: Chemical | ChemComp-NI / #10: Chemical | ChemComp-MG / #11: Chemical | ChemComp-SO4 / #12: Chemical | ChemComp-MES / #13: Chemical | ChemComp-EDO / #14: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.05 Å3/Da / Density % sol: 59.7 % / Description: Thin parallelogram plate |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.6 / Details: 1.5 M magnesium sulfate, 0.1 M MES buffer |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 16, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→200 Å / Num. obs: 245688 / % possible obs: 99.9 % / Redundancy: 14.5 % / Biso Wilson estimate: 24.93 Å2 / Rmerge(I) obs: 0.078 / Χ2: 1.253 / Net I/σ(I): 33.2 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 13.2 % / Rmerge(I) obs: 0.567 / Mean I/σ(I) obs: 6 / Num. unique obs: 24344 / Χ2: 1.439 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5X7O Resolution: 1.95→152.46 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.957 / SU B: 3.391 / SU ML: 0.094 / Cross valid method: THROUGHOUT / ESU R: 0.141 / ESU R Free: 0.129 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.004 Å2
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Refine analyze | Luzzati coordinate error obs: 0.141 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 1.95→152.46 Å
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Refine LS restraints |
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