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Yorodumi- PDB-1fsa: THE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY F... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fsa | ||||||
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Title | THE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI | ||||||
Components | FRUCTOSE 1,6-BISPHOSPHATASE | ||||||
Keywords | HYDROLASE / LYASE / FRUCTOSE 1 / 6-BISPHOSPHATASE / CARBOHYDRATE METABOLISM / GLUCONEOGENESIS / ACETYLATION PHOSPHORYLATION | ||||||
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 / fructose 1,6-bisphosphate metabolic 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 / fructose 1,6-bisphosphate metabolic process / negative regulation of glycolytic process / regulation of gluconeogenesis / AMP binding / dephosphorylation / gluconeogenesis / negative regulation of cell growth / cellular response to xenobiotic stimulus / identical protein binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Lu, G. / Stec, B. / Giroux, E. / Kantrowitz, E.R. | ||||||
Citation | Journal: Protein Sci. / Year: 1996 Title: Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity. Authors: Lu, G. / Stec, B. / Giroux, E.L. / Kantrowitz, E.R. #1: Journal: Protein Sci. / Year: 1996 Title: Crystal Structures of the Active Site Mutant (Arg-243-->Ala) in the T and R Allosteric States of Pig Kidney Fructose-1,6-Bisphosphatase Expressed in Escherichia Coli Authors: Stec, B. / Abraham, R. / Giroux, E. / Kantrowitz, E.R. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose 2,6-Bisphosphate, AMP, and Zn2+ at 2.0-A Resolution: Aspects of Synergism between Inhibitors Authors: Xue, Y. / Huang, S. / Liang, J.Y. / Zhang, Y. / Lipscomb, W.N. #3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1991 Title: Crystal Structure of the Neutral Form of Fructose-1,6-Bisphosphatase Complexed with the Product Fructose 6-Phosphate at 2.1-A Resolution Authors: Ke, H. / Zhang, Y. / Liang, J.Y. / 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 | 1fsa.cif.gz | 143.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fsa.ent.gz | 113.5 KB | Display | PDB format |
PDBx/mmJSON format | 1fsa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/1fsa ftp://data.pdbj.org/pub/pdb/validation_reports/fs/1fsa | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 36645.160 Da / Num. of mol.: 2 / Mutation: K42A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: FBP / Organ: KIDNEY / Plasmid: PEK292 / Gene (production host): FBP / Production host: Escherichia coli (E. coli) / Strain (production host): EK1601 / References: UniProt: P00636, fructose-bisphosphatase #2: Sugar | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.69 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Feb 1, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→80 Å / Num. obs: 27660 / % possible obs: 81 % / Observed criterion σ(I): 0.5 / Redundancy: 2.3 % / Biso Wilson estimate: 30.9 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 3.5 |
Reflection | *PLUS Num. measured all: 66515 |
-Processing
Software |
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Refinement | Resolution: 2.3→10 Å / σ(F): 2 Details: REGIONS WITH WEAK ELECTRON DENSITY AND HIGH TEMPERATURE FACTORS WHICH ARE MOST LIKELY DISORDERED: 1 - 8 AND 64 - 69 IN A AND B SUBUNITS.
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Displacement parameters | Biso mean: 24.31 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.24 Å / Luzzati d res low obs: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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