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Open data
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Basic information
Entry | Database: PDB / ID: 4fua | |||||||||
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Title | L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH | |||||||||
![]() | L-FUCULOSE-1-PHOSPHATE ALDOLASE | |||||||||
![]() | LYASE (ALDEHYDE) / CLASS II ALDOLASE / ZINC ENZYME / HYDROLASE | |||||||||
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: Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. Authors: Dreyer, M.K. / Schulz, G.E. #1: ![]() Title: The 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. #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 KB | Display | ![]() |
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PDB format | ![]() | 41.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.4 KB | Display | ![]() |
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Full document | ![]() | 443.5 KB | Display | |
Data in XML | ![]() | 10.7 KB | Display | |
Data in CIF | ![]() | 14.2 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 23805.318 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: PGH IS A TRANSITION STATE ANALOGUE INHIBITOR / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 70 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/BME.gif)
![](data/chem/img/PGH.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/BME.gif)
![](data/chem/img/PGH.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ZN / |
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#3: Chemical | ChemComp-SO4 / |
#4: Chemical | ChemComp-BME / |
#5: Chemical | ChemComp-PGH / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS 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: 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.13 Å / Num. obs: 10101 / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Rmerge(I) obs: 0.073 |
Reflection | *PLUS Highest resolution: 2.43 Å / Num. obs: 8744 / % possible obs: 85 % / Num. measured all: 50904 |
Reflection shell | *PLUS % possible obs: 47 % |
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Processing
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Refinement | Resolution: 2.43→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 18 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.3 Å / Luzzati sigma a obs: 0.28 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.43→10 Å
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Refine LS restraints |
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