+Open data
-Basic information
Entry | Database: PDB / ID: 2glx | ||||||
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Title | Crystal Structure Analysis of bacterial 1,5-AF Reductase | ||||||
Components | 1,5-anhydro-D-fructose reductase | ||||||
Keywords | OXIDOREDUCTASE / NADP(H) dependent reductase / Rossmann-fold / bacterial 1 / 5-anhydro-D-fructose reductase / sugar metabolism / 1 / 5-anhydro-D-fructose / 5-anhydro-D-mannitol | ||||||
Function / homology | Function and homology information 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) / 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity Similarity search - Function | ||||||
Biological species | Ensifer adhaerens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.2 Å | ||||||
Authors | Dambe, T.R. / Scheidig, A.J. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Crystal Structure of NADP(H)-Dependent 1,5-Anhydro-d-fructose Reductase from Sinorhizobium morelense at 2.2 A Resolution: Construction of a NADH-Accepting Mutant and Its Application in Rare Sugar Synthesis Authors: Dambe, T.R. / Kuehn, A.M. / Brossette, T. / Giffhorn, F. / Scheidig, A.J. #1: Journal: Appl.Environ.Microbiol. / Year: 2006 Title: Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar ...Title: Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis Authors: Kuehn, A.M. / Yu, S. / Giffhorn, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2glx.cif.gz | 403.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2glx.ent.gz | 330.7 KB | Display | PDB format |
PDBx/mmJSON format | 2glx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gl/2glx ftp://data.pdbj.org/pub/pdb/validation_reports/gl/2glx | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 34975.246 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Ensifer adhaerens (bacteria) / Strain: S-30.7.5 / Gene: afr / Plasmid: pET24a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q2I8V6, EC: 1.1.1.263 #2: Chemical | ChemComp-ACT / #3: Chemical | ChemComp-NDP / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.95 Å3/Da / Density % sol: 58.29 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 100mM NaCitrat, 200mM Ammoniumacetat, 30% MPEG 5000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 2.2→19 Å / Num. all: 123108 / Num. obs: 123108 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 38.236 Å2 / Rmerge(I) obs: 0.124 / Rsym value: 0.124 / Net I/σ(I): 8.56 | ||||||||||||||||||
Reflection shell | Resolution: 2.2→2.3 Å / % possible obs: 96.4 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.437 / Mean I/σ(I) obs: 3.6 / Num. measured obs: 52622 / Num. unique all: 15426 / Num. unique obs: 14875 / Rsym value: 0.448 / % possible all: 0.99 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.2→19 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.921 / SU B: 6.687 / SU ML: 0.166 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.24 / ESU R Free: 0.21 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.652 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→19 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.256 Å / Total num. of bins used: 20
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