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- PDB-6mnu: Crystal structure of Yersinia pestis UDP-glucose pyrophosphorylase -
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Open data
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Basic information
Entry | Database: PDB / ID: 6mnu | ||||||
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Title | Crystal structure of Yersinia pestis UDP-glucose pyrophosphorylase | ||||||
![]() | UTP--glucose-1-phosphate uridylyltransferase | ||||||
![]() | TRANSFERASE / UDP-glucose pyrophosphorylase / plague / Yersinia pestis | ||||||
Function / homology | ![]() UTP-glucose-1-phosphate uridylyltransferase / UTP:glucose-1-phosphate uridylyltransferase activity / UDP-glucose metabolic process / biosynthetic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gibbs, M.E. / Lountos, G.T. / Gumpena, R. / Waugh, D.S. | ||||||
![]() | ![]() Title: Crystal structure of UDP-glucose pyrophosphorylase from Yersinia pestis, a potential therapeutic target against plague. Authors: Gibbs, M.E. / Lountos, G.T. / Gumpena, R. / Waugh, D.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 236.4 KB | Display | ![]() |
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PDB format | ![]() | 189.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 461.3 KB | Display | ![]() |
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Full document | ![]() | 468.6 KB | Display | |
Data in XML | ![]() | 46.4 KB | Display | |
Data in CIF | ![]() | 67.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2e3dS 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: 32308.621 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: galU, galU1, y2631, YP_1428, DBB30_10560, EGT45_14485, NCTC144_03080 Plasmid: pMG3038 / Production host: ![]() ![]() References: UniProt: A0A2S9PFH5, UniProt: A0A3N4B738*PLUS, UTP-glucose-1-phosphate uridylyltransferase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 46.15 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 0.1M MES pH 6.0 20% PEG Low Smear (PEG 1000, PEG400, PEG600, PEG MME 500), 10 mM spermidine |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300-HS / Detector: CCD / Date: Aug 5, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→50 Å / Num. obs: 61347 / % possible obs: 97.6 % / Redundancy: 4.6 % / Rpim(I) all: 0.041 / Rrim(I) all: 0.09 / Rsym value: 0.08 / Net I/σ(I): 17.1 |
Reflection shell | Resolution: 2.17→2.21 Å / Redundancy: 4.2 % / Mean I/σ(I) obs: 2.1 / Num. unique obs: 3054 / CC1/2: 0.774 / Rpim(I) all: 0.343 / Rrim(I) all: 0.722 / Rsym value: 0.631 / % possible all: 99.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2E3D Resolution: 2.172→26.709 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.38
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.172→26.709 Å
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Refine LS restraints |
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LS refinement shell |
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