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- PDB-5nzl: Crystal structure of UDP-glucose pyrophosphorylase from Leishmani... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5nzl | ||||||
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Title | Crystal structure of UDP-glucose pyrophosphorylase from Leishmania major in complex with resveratrol | ||||||
![]() | UDP-glucose pyrophosphorylase | ||||||
![]() | TRANSFERASE / NTP-transferase / Pathogen / Allostery / Catalysis | ||||||
Function / homology | ![]() UTP-glucose-1-phosphate uridylyltransferase / UTP:glucose-1-phosphate uridylyltransferase activity / UDP-alpha-D-glucose metabolic process / ciliary plasm / nuclear lumen / glycogen metabolic process / cytosol / cytoplasm 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 | ![]() | 110.2 KB | Display | ![]() |
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PDB format | ![]() | 83.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 460.9 KB | Display | ![]() |
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Full document | ![]() | 467.9 KB | Display | |
Data in XML | ![]() | 20 KB | Display | |
Data in CIF | ![]() | 27.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5nzgC ![]() 5nzhC ![]() 5nziC ![]() 5nzjC ![]() 5nzkC ![]() 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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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 56054.770 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q4QDU3, UTP-glucose-1-phosphate uridylyltransferase | ||
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#2: Chemical | ChemComp-STL / | ||
#3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.18 % / Mosaicity: 0.252 ° |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop Details: 2.25 M ammonium sulfate, 100 mM 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: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 28, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 24020 / % possible obs: 99.9 % / Redundancy: 5.84 % / Biso Wilson estimate: 41.9 Å2 / Rsym value: 0.042 / Net I/σ(I): 15.95 |
Reflection shell | Mean I/σ(I) obs: 2.14 / Num. unique obs: 2733 / Rsym value: 0.455 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2OEF Resolution: 2.4→47.357 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.25
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→47.357 Å
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Refine LS restraints |
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LS refinement shell |
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