+Open data
-Basic information
Entry | Database: PDB / ID: 3e3p | ||||||
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Title | Glycogen synthase kinase from Leishmania major | ||||||
Components | Protein kinase, putative Glycogen synthase kinase | ||||||
Keywords | TRANSFERASE / glycogen synthase kinase / leishmaniasis / Kinase | ||||||
Function / homology | Function and homology information ciliary tip / nuclear lumen / ciliary plasm / non-specific serine/threonine protein kinase / protein serine/threonine kinase activity / signal transduction / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Leishmania major (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å | ||||||
Authors | Arakaki, T.L. / Merritt, E.A. | ||||||
Citation | Journal: To be Published Title: Glycogen synthase kinase from Leishmania major Authors: Arakaki, T.L. / Merritt, E.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3e3p.cif.gz | 146.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3e3p.ent.gz | 115.8 KB | Display | PDB format |
PDBx/mmJSON format | 3e3p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e3/3e3p ftp://data.pdbj.org/pub/pdb/validation_reports/e3/3e3p | HTTPS FTP |
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-Related structure data
Related structure data | |
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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
#1: Protein | Mass: 41198.332 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Lmaj002314AAA LmjF18.0270 / Source: (gene. exp.) Leishmania major (eukaryote) / Gene: LmjF18.0270 / Plasmid: AVA421 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3 / References: UniProt: Q4QE15, EC: 2.7.1.37 #2: 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 |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 7 Details: 70% Tacsimate, 0.1 M Bis Tris propane, pH 7.0, vapor diffusion, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.9184 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 22, 2007 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2→50 Å / Num. obs: 54336 / % possible obs: 92.3 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.087 / Χ2: 1.122 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→40 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.932 / WRfactor Rfree: 0.278 / WRfactor Rwork: 0.224 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.695 / SU B: 7.946 / SU ML: 0.202 / SU R Cruickshank DPI: 0.206 / SU Rfree: 0.187 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.206 / ESU R Free: 0.187 / 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: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 82.22 Å2 / Biso mean: 46.061 Å2 / Biso min: 17.56 Å2
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Refinement step | Cycle: LAST / Resolution: 2→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.003→2.055 Å / Total num. of bins used: 20
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