+Open data
-Basic information
Entry | Database: PDB / ID: 6b65 | ||||||
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Title | IMPase (AF2372) R92Q/K164E | ||||||
Components | Fructose-1,6-bisphosphatase/inositol-1-monophosphatase | ||||||
Keywords | HYDROLASE / Osmolyte binding protein / inositol monophosphatase | ||||||
Function / homology | Function and homology information inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / phosphatidylinositol phosphate biosynthetic process / carbohydrate metabolic process / metal ion binding Similarity search - Function | ||||||
Biological species | Archaeoglobus fulgidus (archaea) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.702 Å | ||||||
Authors | Goldstein, R.I. / Roberts, M. | ||||||
Funding support | United States, 1items
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Citation | Journal: To Be Published 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6b65.cif.gz | 113.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6b65.ent.gz | 86.7 KB | Display | PDB format |
PDBx/mmJSON format | 6b65.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b6/6b65 ftp://data.pdbj.org/pub/pdb/validation_reports/b6/6b65 | HTTPS FTP |
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-Related structure data
Related structure data | 6b5zC 6b60C 6b61C 6b62C 6b63C 6b64C 6b66C 1lvbS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 27973.705 Da / Num. of mol.: 2 / Mutation: R92Q, K164E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) (archaea) Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126 Gene: suhB, AF_2372 / Production host: Escherichia coli (E. coli) References: UniProt: O30298, fructose-bisphosphatase, inositol-phosphate phosphatase |
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-Non-polymers , 5 types, 82 molecules
#2: Chemical | #3: Chemical | ChemComp-MG / #4: Chemical | #5: Chemical | #6: 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: 4.27 Å3/Da / Density % sol: 71.18 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 100 mM myo inositol 14% PEG 3350 200 mM potassium sulfate 100 mM magnesium chloride 100 mM Hepes 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Aug 31, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→36.48 Å / Num. obs: 24448 / % possible obs: 96.48 % / Redundancy: 5.2 % / Net I/σ(I): 2.776 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1LVB Resolution: 2.702→36.48 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 29.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.702→36.48 Å
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Refine LS restraints |
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LS refinement shell |
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