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Open data
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Basic information
Entry | Database: PDB / ID: 1zen | ||||||
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Title | CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE | ||||||
![]() | CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE | ||||||
![]() | LYASE / ALDEHYDE / GLYCOLYSIS | ||||||
Function / homology | ![]() fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / gluconeogenesis / glycolytic process / protein homodimerization activity / zinc ion binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Cooper, S.J. / Leonard, G.A. / Hunter, W.N. | ||||||
![]() | ![]() Title: The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. Authors: Cooper, S.J. / Leonard, G.A. / McSweeney, S.M. / Thompson, A.W. / Naismith, J.H. / Qamar, S. / Plater, A. / Berry, A. / Hunter, W.N. #1: ![]() Title: Identification of Arginine 331 as an Important Active Site Residue in the Class II Fructose-1,6-Bisphosphate Aldolase of Escherichia Coli Authors: Qamar, S. / Marsh, K. / Berry, A. #2: ![]() Title: Identification of Zinc Binding Ligands in the Class II Fructose-1,6-Bisphosphate Aldolase of Escherichia Coli Authors: Berry, A. / Marshall, K.E. #3: ![]() Title: Initiating a Crystallographic Study of a Class II Fructose-1,6-Bisphosphate Aldolase Authors: Naismith, J.H. / Ferrara, J.D. / Bailey, S. / Marshall, K. / Dauter, Z. / Wilson, K.S. / Habash, J. / Harrop, S.J. / Berry, A.J. / Hunter, W.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.2 KB | Display | ![]() |
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PDB format | ![]() | 58.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.9 KB | Display | ![]() |
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Full document | ![]() | 429.5 KB | Display | |
Data in XML | ![]() | 16 KB | Display | |
Data in CIF | ![]() | 21.4 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 39059.957 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.29 Å3/Da / Density % sol: 62.64 % | ||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, hanging drop / Details: Kitagawa, Y., (1995) Acta Cryst. D., 51, 833. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07 Å / Relative weight: 1 |
Reflection | Num. obs: 18922 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.071 |
Reflection | *PLUS Highest resolution: 2.5 Å / % possible obs: 98 % |
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Processing
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Refinement | Resolution: 2.5→6 Å / σ(F): 4
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Displacement parameters | Biso mean: 35.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.6 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.3269 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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