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Yorodumi- PDB-1fpk: FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPH... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fpk | ||||||
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Title | FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH THALLIUM IONS (10 MM) | ||||||
Components | FRUCTOSE-1,6-BISPHOSPHATASE | ||||||
Keywords | HYDROLASE (PHOSPHORIC MONOESTER) / HYDROLASE / PHOSPHORIC MONOESTER / CARBOHYDRATE METABOLISM | ||||||
Function / homology | Function and homology information 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 | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Villeret, V. / Lipscomb, W.N. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1995 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: Journal: Biochemistry / Year: 1995 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: Journal: Biochem.Biophys.Res.Commun. / Year: 1993 Title: Structural Similarities between Fructose-1,6-Bisphosphatase and Inositol Monophosphatase Authors: Zhang, Y. / Liang, J.-Y. / Lipscomb, W.N. #3: Journal: Biochemistry / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fpk.cif.gz | 128.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fpk.ent.gz | 102.5 KB | Display | PDB format |
PDBx/mmJSON format | 1fpk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fpk_validation.pdf.gz | 377.3 KB | Display | wwPDB validaton report |
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Full document | 1fpk_full_validation.pdf.gz | 393.2 KB | Display | |
Data in XML | 1fpk_validation.xml.gz | 15.1 KB | Display | |
Data in CIF | 1fpk_validation.cif.gz | 22.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fp/1fpk ftp://data.pdbj.org/pub/pdb/validation_reports/fp/1fpk | HTTPS FTP |
-Related structure data
-Links
-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 - 6 AND 55 - 71 WERE OMITTED IN THE MODEL DUE TO A LACK OF WELL-DEFINED ELECTRON DENSITY. |
-Components
#1: Protein | Mass: 36503.004 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: KIDNEY / References: UniProt: P00636, fructose-bisphosphatase #2: Chemical | ChemComp-TL / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.71 % | ||||||||||||||||||||
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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: Dec 17, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→15 Å / Num. obs: 14091 / % possible obs: 74 % / Redundancy: 2.41 % / Rmerge(I) obs: 0.091 |
Reflection | *PLUS Num. measured all: 33304 |
-Processing
Software |
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Refinement | Resolution: 3→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 31.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |