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Open data
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Basic information
Entry | Database: PDB / ID: 6b61 | ||||||
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Title | IMPase (AF2372) with 25 mM Asp | ||||||
![]() | Fructose-1,6-bisphosphatase/inositol-1-monophosphatase | ||||||
![]() | HYDROLASE / Osmolyte binding protein / inositol monophosphatase | ||||||
Function / homology | ![]() inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / inositol metabolic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / phosphatidylinositol phosphate biosynthetic process / signal transduction / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Goldstein, R.I. / Roberts, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Osmolyte binding capacity of a dual action IMPase/FBPase (AF2372) Authors: Goldstein, R.I. / Roberts, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 116.2 KB | Display | ![]() |
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PDB format | ![]() | 88.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.2 MB | Display | ![]() |
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Full document | ![]() | 3.3 MB | Display | |
Data in XML | ![]() | 22.5 KB | Display | |
Data in CIF | ![]() | 30.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6b5zC ![]() 6b60C ![]() 6b62C ![]() 6b63C ![]() 6b64C ![]() 6b65C ![]() 6b66C ![]() 1lvbS S: Starting model for refinement C: citing same article ( |
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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: 28002.838 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126 Gene: suhB, AF_2372 / Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-ASP / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.24 Å3/Da / Density % sol: 70.98 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 100 mM myo inositol 400 mM Aspartate 12 % PEG 3350 200 mM Potassium Sulfate 100 mM Magnesium Chloride 100 mM HEPES pH7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Nov 18, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→44.75 Å / Num. obs: 62169 / % possible obs: 99.98 % / Redundancy: 2.6 % / Net I/σ(I): 2.161 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1LVB Resolution: 2.7→42.731 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.97 / Phase error: 21.9
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Solvent computation | Shrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Bsol: 34.576 Å2 / ksol: 0.386 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.7→42.731 Å
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Refine LS restraints |
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LS refinement shell |
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