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- PDB-6a0l: Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from Arthrobacter... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6a0l | |||||||||
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Title | Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from Arthrobacter globiformis, complex with maltose | |||||||||
![]() | Cyclic maltosyl-maltose hydrolase | |||||||||
![]() | HYDROLASE | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Kohno, M. / Arakawa, T. / Mori, T. / Nishimoto, T. / Fushinobu, S. | |||||||||
![]() | ![]() Title: Structural features of a bacterial cyclic alpha-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis. Authors: Kohno, M. / Arakawa, T. / Ota, H. / Mori, T. / Nishimoto, T. / Fushinobu, S. #1: Journal: Biosci. Biotechnol. Biochem. / Year: 2008 Title: Purification and characterization of cyclic maltosyl-(1-->6)-maltose hydrolase and alpha-glucosidase from an Arthrobacter globiformis strain. Authors: Mori, T. / Nishimoto, T. / Okura, T. / Chaen, H. / Fukuda, S. #2: ![]() Title: Cloning, Sequencing and Expression of the Genes Encoding Cyclic alpha-Maltosyl-(1-->6)-maltose Hydrolase and alpha-Glucosidase from an Arthrobacter globiformis Strain Authors: Mori, T. / Nishimoto, T. / Okura, T. / Chaen, H. / Fukuda, S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 104.5 KB | Display | ![]() |
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PDB format | ![]() | 75.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 816.6 KB | Display | ![]() |
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Full document | ![]() | 823.7 KB | Display | |
Data in XML | ![]() | 18.5 KB | Display | |
Data in CIF | ![]() | 26.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5zxgSC ![]() 6a0jC ![]() 6a0kC 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: 51664.258 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.68 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 0.1 M Sodium citrte, 0.22 M Ammonium sulfate, 30% (w/v) PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Nov 5, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→91.1 Å / Num. obs: 26693 / % possible obs: 88.6 % / Redundancy: 4 % / Rmerge(I) obs: 0.141 / Net I/σ(I): 0.115 |
Reflection shell | Resolution: 2.1→2.14 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.552 / Mean I/σ(I) obs: 0.022 / Num. unique obs: 25316 / CC1/2: 0.839 / % possible all: 96.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5ZXG Resolution: 2.1→91.1 Å / Cor.coef. Fo:Fc: 0.923 / Cor.coef. Fo:Fc free: 0.85 / SU B: 9.368 / SU ML: 0.235 / Cross valid method: THROUGHOUT / ESU R: 0.317 / ESU R Free: 0.269 / 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: 31.529 Å2
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Refinement step | Cycle: 1 / Resolution: 2.1→91.1 Å
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Refine LS restraints |
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