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Open data
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Basic information
Entry | Database: PDB / ID: 1fua | ||||||
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Title | L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T | ||||||
![]() | L-FUCULOSE-1-PHOSPHATE ALDOLASE | ||||||
![]() | LYASE (ALDEHYDE) / CLASS II ALDOLASE / ZINC ENZYME | ||||||
Function / homology | ![]() L-fuculose-phosphate aldolase / L-fuculose-phosphate aldolase activity / D-arabinose catabolic process / L-fucose catabolic process / pentose catabolic process / aldehyde-lyase activity / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Dreyer, M.K. / Schulz, G.E. | ||||||
![]() | ![]() Title: Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli. Authors: Dreyer, M.K. / Schulz, G.E. #1: ![]() Title: Catalytic Mechanism of the Metal-Dependent Fuculose Aldolase from Escherichia Coli as Derived from the Structure Authors: Dreyer, M.K. / Schulz, G.E. #2: ![]() Title: The Spatial Structure of the Class II L-Fuculose-1-Phosphate Aldolase from Escherichia Coli Authors: Dreyer, M.K. / Schulz, G.E. #3: ![]() Title: Diastereoselective Enzymatic Aldol Additions: L-Rhamnulose and L-Fuculose 1-Phosphate Aldolases from E.Coli Authors: Fessner, W.-D. / Sinerius, G. / Schneider, A. / Dreyer, M. / Schulz, G.E. / Badia, J. / Aguilar, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.9 KB | Display | ![]() |
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PDB format | ![]() | 40.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.9 KB | Display | ![]() |
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Full document | ![]() | 434.7 KB | Display | |
Data in XML | ![]() | 11 KB | Display | |
Data in CIF | ![]() | 14.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
#1: Protein | Mass: 23805.318 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: PH 7.8 / Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-ZN / | ||||
#3: Chemical | #4: Chemical | ChemComp-BME / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 38 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.8 / Details: pH 7.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 7.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.62 Å / Num. obs: 19917 / Observed criterion σ(I): 0 / Redundancy: 9.1 % / Rmerge(I) obs: 0.065 |
Reflection | *PLUS Highest resolution: 1.92 Å / Lowest resolution: 10 Å / % possible obs: 97 % |
Reflection shell | *PLUS Highest resolution: 1.92 Å / Lowest resolution: 1.96 Å / % possible obs: 93 % / Rmerge(I) obs: 0.284 |
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Processing
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Refinement | Resolution: 1.92→10 Å / σ(F): 0 Details: THE OCCUPANCY OF SULFATE ION 301 WAS REFINED TO 0.71.
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Displacement parameters | Biso mean: 19 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.22 Å / Luzzati sigma a obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.92→10 Å
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Refine LS restraints |
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