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- PDB-4km4: E. coli alkaline phosphatase mutant S102G/R166S in complex with i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4km4 | ||||||
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Title | E. coli alkaline phosphatase mutant S102G/R166S in complex with inorganic phosphate | ||||||
![]() | Alkaline phosphatase | ||||||
![]() | HYDROLASE / Phosphate Monoester Hydrolase / periplasmic | ||||||
Function / homology | ![]() oxidoreductase activity, acting on phosphorus or arsenic in donors / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / dephosphorylation / protein dephosphorylation / outer membrane-bounded periplasmic space / periplasmic space / magnesium ion binding / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Andrews, L.D. / Fenn, T.D. / Herschlag, D. | ||||||
![]() | ![]() Title: Ground state destabilization by anionic nucleophiles contributes to the activity of phosphoryl transfer enzymes. Authors: Andrews, L.D. / Fenn, T.D. / Herschlag, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 297.6 KB | Display | ![]() |
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PDB format | ![]() | 250.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.2 KB | Display | ![]() |
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Full document | ![]() | 454 KB | Display | |
Data in XML | ![]() | 30.3 KB | Display | |
Data in CIF | ![]() | 41.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1alkS S: Starting model for refinement |
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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: 46537.742 Da / Num. of mol.: 2 / Mutation: S102G, R166S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-ZN / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.11 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8 Details: Equal parts 23.5 mg/mL enzyme in 10 mM NaMOPS and 50 mM NaCl and 0.2 M NH4F, 17-21% PEG 3350, and 500 uM ZnCl2, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Jun 6, 2011 |
Radiation | Monochromator: Double crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. obs: 26488 / % possible obs: 99.21 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 20.4 % / Rmerge(I) obs: 0.337 / Rsym value: 0.41 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 2.8→2.91 Å / Mean I/σ(I) obs: 3.9 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ALK Resolution: 2.8→50 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→50 Å
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