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Open data
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Basic information
Entry | Database: PDB / ID: 4d3p | ||||||
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Title | crystal structure of point mutated DUSP19 (C150A) | ||||||
![]() | DUAL SPECIFICITY PROTEIN PHOSPHATASE 19 | ||||||
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Function / homology | ![]() JUN kinase phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / negative regulation of JUN kinase activity / MAP-kinase scaffold activity / negative regulation of JNK cascade / mitogen-activated protein kinase kinase kinase binding / myosin phosphatase activity / protein-serine/threonine phosphatase / ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Jeon, T.J. / Nam, K.T. / Ryu, S.E. | ||||||
![]() | ![]() Title: Structural Analysis of Activity-Modulating Mutations of Dusp19 Authors: Jeon, T.J. / Nam, K.T. / Ryu, S.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 47.3 KB | Display | ![]() |
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PDB format | ![]() | 32.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4d3qC ![]() 4d3rC ![]() 3s4eS C: citing same article ( 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: 16203.410 Da / Num. of mol.: 1 / Fragment: PHOSPHATASE DOMAINS, UNP RESIDUES 65-205 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: Q8WTR2, protein-serine/threonine phosphatase, ![]() | ||
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#2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.96 % / Description: NONE |
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Crystal grow![]() | Details: 1.8M AMMONIUM SULFATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 6, 2013 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.18→50 Å / Num. obs: 45782 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 7.1 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.8 |
Reflection shell | Resolution: 1.18→1.2 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 5.6 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 3S4E Resolution: 1.27→6 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.958 / SU B: 0.516 / SU ML: 0.024 / Cross valid method: THROUGHOUT / ESU R: 0.043 / ESU R Free: 0.045 / 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: 8.807 Å2
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Refinement step | Cycle: LAST / Resolution: 1.27→6 Å
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Refine LS restraints |
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