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- PDB-1fpi: FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPH... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fpi | ||||||
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Title | FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND POTASSIUM IONS (100 MM) | ||||||
![]() | FRUCTOSE-1,6-BISPHOSPHATASE | ||||||
![]() | HYDROLASE (PHOSPHORIC MONOESTER) / HYDROLASE / PHOSPHORIC MONOESTER / CARBOHYDRATE METABOLISM | ||||||
Function / homology | ![]() Gluconeogenesis / sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / cellular response to magnesium ion / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process / fructose metabolic process / monosaccharide binding / negative regulation of glycolytic process ...Gluconeogenesis / sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / cellular response to magnesium ion / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process / fructose metabolic process / monosaccharide binding / negative regulation of glycolytic process / fructose 1,6-bisphosphate metabolic process / regulation of gluconeogenesis / AMP binding / dephosphorylation / gluconeogenesis / negative regulation of cell growth / cellular response to xenobiotic stimulus / identical protein binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Villeret, V. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase. Authors: Villeret, V. / Huang, S. / Fromm, H.J. / Lipscomb, W.N. #1: ![]() Title: Structural Aspects of the Allosteric Inhibition of Fructose-1,6-Bisphosphatase by AMP: The Binding of Both the Substrate Analogue 2,5-Anhydro-D-Glucitol 1,6-Bisphosphate and Catalytic Metal ...Title: Structural Aspects of the Allosteric Inhibition of Fructose-1,6-Bisphosphatase by AMP: The Binding of Both the Substrate Analogue 2,5-Anhydro-D-Glucitol 1,6-Bisphosphate and Catalytic Metal Ions Monitored by X-Ray Crystallography Authors: Villeret, V. / Huang, S. / Zhang, Y. / Lipscomb, W.N. #2: ![]() Title: Structural Similarities between Fructose-1,6-Bisphosphatase and Inositol Monophosphatase Authors: Zhang, Y. / Liang, J.Y. / Lipscomb, W.N. #3: ![]() Title: Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase Authors: Zhang, Y. / Liang, J.Y. / Huang, S. / Ke, H. / Lipscomb, 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 | ![]() | 136.6 KB | Display | ![]() |
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PDB format | ![]() | 107.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 569.5 KB | Display | ![]() |
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Full document | ![]() | 581 KB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 22.7 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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Details | THERE ARE TWO MONOMERS IN THE ASYMMETRIC UNIT, WHICH IS HALF THE MOLECULE. RESIDUES 1 - 8 AND 62 - 71 WERE OMITTED IN THE MODEL DUE TO A LACK OF WELL-DEFINED ELECTRON DENSITY. |
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Components
#1: Protein | Mass: 36503.004 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | ChemComp-K / #3: Chemical | #4: Sugar | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.08 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: microdialysis | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Date: Feb 27, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→15 Å / Num. obs: 31345 / % possible obs: 89 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.072 |
Reflection | *PLUS Num. obs: 29101 / % possible obs: 83 % / Num. measured all: 98031 |
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Processing
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Refinement | Resolution: 2.3→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 24.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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