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- PDB-5nzh: Crystal structure of UDP-glucose pyrophosphorylase V402W mutant f... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5nzh | ||||||
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Title | Crystal structure of UDP-glucose pyrophosphorylase V402W mutant from Leishmania major | ||||||
![]() | UDP-glucose pyrophosphorylase | ||||||
![]() | TRANSFERASE / NTP-transferase / Pathogen / Allostery / Catalysis | ||||||
Function / homology | ![]() UTP-glucose-1-phosphate uridylyltransferase / UTP:glucose-1-phosphate uridylyltransferase activity / UDP-glucose metabolic process / nuclear lumen / ciliary plasm / glycogen metabolic process / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cramer, J.T. / Fuehring, J.I. / Baruch, P. / Bruetting, C. / Hesse, R. / Knoelker, H.-J. / Gerardy-Schahn, R. / Fedorov, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Decoding Allosteric Networks in Biocatalysts: Rational Approach to Therapies and Biotechnologies Authors: Cramer, J.T. / Fuehring, J.I. / Baruch, P. / Bruetting, C. / Knoelker, H.-J. / Gerardy-Schahn, R. / Fedorov, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 203.4 KB | Display | ![]() |
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PDB format | ![]() | 162.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.8 KB | Display | ![]() |
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Full document | ![]() | 462.6 KB | Display | |
Data in XML | ![]() | 38.6 KB | Display | |
Data in CIF | ![]() | 54.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5nzgC ![]() 5nziC ![]() 5nzjC ![]() 5nzkC ![]() 5nzlC ![]() 5nzmC ![]() 2oefS 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 56141.852 Da / Num. of mol.: 2 / Mutation: V402W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q4QDU3, UTP-glucose-1-phosphate uridylyltransferase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.63 % / Mosaicity: 0.32 ° |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop Details: 2.25M ammonium sulfate, 100mM Tris-HCl pH 7.2, 0.1% Tween 80 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 25, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.03 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→47.854 Å / Num. obs: 26339 / % possible obs: 99.9 % / Redundancy: 7.04 % / Biso Wilson estimate: 21.83 Å2 / Rsym value: 0.0183 / Net I/σ(I): 4.37 |
Reflection shell | Mean I/σ(I) obs: 2.14 / Rsym value: 0.46 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2OEF Resolution: 2.9→47.854 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 27.58
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→47.854 Å
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Refine LS restraints |
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LS refinement shell |
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