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Open data
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Basic information
Entry | Database: PDB / ID: 1ado | ||||||
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Title | FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE | ||||||
![]() | ALDOLASE | ||||||
![]() | LYASE / ALDOLASE / LYASE (ALDEHYDE) / SCHIFF BASE / GLYCOLYSIS | ||||||
Function / homology | ![]() negative regulation of Arp2/3 complex-mediated actin nucleation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / I band / fructose 1,6-bisphosphate metabolic process / glycolytic process / protein homotetramerization / positive regulation of cell migration / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Blom, N.S. / Sygusch, J. | ||||||
![]() | ![]() Title: Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase. Authors: Blom, N. / Sygusch, J. #1: ![]() Title: Enhanced Electron Density Envelopes by Extended Solvent Definition Authors: Blom, N.S. / Sygusch, 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 | ![]() | 417.8 KB | Display | ![]() |
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PDB format | ![]() | 335.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417.5 KB | Display | ![]() |
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Full document | ![]() | 438.1 KB | Display | |
Data in XML | ![]() | 30.5 KB | Display | |
Data in CIF | ![]() | 64.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 39253.637 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % | |||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: RABBIT MUSCLE ALDOLASE WAS CRYSTALLIZED FROM A 42% SATURATED AMMONIUM SULFATE SOLUTION, pH 7.5 | |||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.3 / Method: unknown / Details: Eagles, P. A., (1969) J. Mol. Biol., 45, 533-544 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Oct 1, 1991 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→12 Å / Num. obs: 103662 / % possible obs: 85.2 % / Observed criterion σ(I): 1 / Rsym value: 0.056 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 1.9→2 Å / Mean I/σ(I) obs: 1.9 / Rsym value: 0.286 |
Reflection | *PLUS Rmerge(I) obs: 0.056 |
Reflection shell | *PLUS Rmerge(I) obs: 0.286 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: STRUCTURE TO 2.7 ANGSTROM RESOLUTION Resolution: 1.9→12 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1
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Displacement parameters | Biso mean: 29.1 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.99 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.262 |