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- PDB-4as3: Pseudomonas Aeruginosa Phosphorylcholine Phosphatase. Orthorhombi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4as3 | ||||||
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Title | Pseudomonas Aeruginosa Phosphorylcholine Phosphatase. Orthorhombic form | ||||||
![]() | PHOSPHORYLCHOLINE PHOSPHATASE | ||||||
![]() | HYDROLASE / HAD SUPERFAMILY / ALKYLAMMONIUM COMPOUNDS | ||||||
Function / homology | ![]() phosphoethanolamine/phosphocholine phosphatase / periplasmic space / hydrolase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Infantes, L. / Otero, L.H. / Albert, A. | ||||||
![]() | ![]() Title: The Structural Domains of Pseudomonas Aeruginosa Phosphorylcholine Phosphatase Cooperate in Substrate Hydrolysis: 3D Structure and Enzymatic Mechanism. Authors: Infantes, L. / Otero, L.H. / Beassoni, P.R. / Boetsch, C. / Lisa, A.T. / Domenech, C.E. / Albert, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 277.4 KB | Display | ![]() |
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PDB format | ![]() | 226.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.5 KB | Display | ![]() |
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Full document | ![]() | 497.1 KB | Display | |
Data in XML | ![]() | 55.1 KB | Display | |
Data in CIF | ![]() | 75 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4as2SC 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 37131.242 Da / Num. of mol.: 4 / Fragment: RESIDUES 23-349 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9HTR2, phosphoethanolamine/phosphocholine phosphatase #2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-CL / #4: Chemical | ChemComp-BTB / #5: Water | ChemComp-HOH / | Sequence details | 22 FIRST AMINOACIDS | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.41 % / Description: NONE |
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Crystal grow | Details: 1UL PROTEIN SOLUTION (10 MG ML-1) WAS MIXED WITH 2UL PRECIPITANT SOLUTION (0.1 M BIS-TRIS PH 5.5, 0.2 M MGCL2, 25% PEG 3350) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 5, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.747091 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50.05 Å / Num. obs: 54739 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 8.4 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 20.7 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 7.8 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 4.9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4AS2 Resolution: 2.4→119.6 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.918 / SU B: 7.464 / SU ML: 0.165 / Cross valid method: THROUGHOUT / ESU R: 0.109 / ESU R Free: 0.059 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.779 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→119.6 Å
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Refine LS restraints |
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