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Open data
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Basic information
Entry | Database: PDB / ID: 1bd4 | ||||||
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Title | UPRT-URACIL COMPLEX | ||||||
![]() | URACIL PHOSPHORIBOSYLTRANSFERASE | ||||||
![]() | TRANSFERASE / UPRT / URACIL / GLYCOSYLTRANSFERASE / COMPLEX | ||||||
Function / homology | ![]() ribosylnicotinamide kinase activity / uracil phosphoribosyltransferase / uracil phosphoribosyltransferase activity / UMP salvage / chloroplast / GTP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schumacher, M.A. / Carter, D. / Scott, D. / Roos, D. / Ullman, B. / Brennan, R.G. | ||||||
![]() | ![]() Title: Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding. Authors: Schumacher, M.A. / Carter, D. / Scott, D.M. / Roos, D.S. / Ullman, B. / Brennan, R.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.6 KB | Display | ![]() |
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PDB format | ![]() | 153.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.1 KB | Display | ![]() |
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Full document | ![]() | 496.1 KB | Display | |
Data in XML | ![]() | 27.9 KB | Display | |
Data in CIF | ![]() | 41 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
#1: Protein | Mass: 27558.246 Da / Num. of mol.: 4 / Mutation: C128V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q26998, uracil phosphoribosyltransferase #2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-URA / #4: Water | ChemComp-HOH / | Nonpolymer details | THE STRUCTURE HAS TWO PHOSPHATE MOLECULES (USED IN CRYSTALLIZATION). ONE PHOSPHATE FOUND IN THE ...THE STRUCTURE HAS TWO PHOSPHATE MOLECULES (USED IN CRYSTALLIZ | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.14 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 49 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Detector | Date: Jan 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 2.2 Å |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 10 Å / Num. obs: 53303 / % possible obs: 87 % / Num. measured all: 111427 / Rmerge(I) obs: 0.052 |
Reflection shell | *PLUS Highest resolution: 2.16 Å / Lowest resolution: 2.23 Å / Mean I/σ(I) obs: 3.9 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.2→10 Å / σ(F): 1 Details: THERE IS A TETRAMER (CHAINS A, B, C, D) IN THE ASYMMETRIC UNIT. THERE ARE FOUR IN THE ASYMMETRIC UNIT FOR SPACE GROUP P21. P21 SPACE GROUP CAN BE TRANSFORMED TO C2221. SOLVED AS P21 FOR ...Details: THERE IS A TETRAMER (CHAINS A, B, C, D) IN THE ASYMMETRIC UNIT. THERE ARE FOUR IN THE ASYMMETRIC UNIT FOR SPACE GROUP P21. P21 SPACE GROUP CAN BE TRANSFORMED TO C2221. SOLVED AS P21 FOR TECHNICAL REASONS. THE N-TERMINAL MET IS CLEAVED OFF IN ESCHERICHIA COLI. RESIDUES 2 THROUGH 20 ARE DISORDERED AND NOT INCLUDED. STRUCTURE INCLUDES RESIDUES 21 TO 244 OF EACH MONOMER. THERE IS A TETRAMER (CHAINS A, B, C, D) IN THE ASYMMETRIC UNIT. THERE ARE FOUR IN THE ASYMMETRIC UNIT FOR SPACE GROUP P21. P21 SPACE GROUP CAN BE TRANSFORMED TO C2221. SOLVED AS P21 FOR TECHNICAL REASONS.
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.181 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |