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Open data
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Basic information
Entry | Database: PDB / ID: 1k0d | ||||||
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Title | Ure2p in Complex with Glutathione | ||||||
![]() | URE2 PROTEIN | ||||||
![]() | GENE REGULATION / Nitrate assimilation / Structural genomics | ||||||
Function / homology | ![]() Oxidoreductases; Acting on a sulfur group of donors; With a disulfide as acceptor / protein urmylation / glutathione peroxidase / negative regulation of transcription by transcription factor localization / regulation of nitrogen utilization / glutathione peroxidase activity / nitrate assimilation / phosphoprotein binding / transcription corepressor activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bousset, L. / Belrhali, H. / Melki, R. / Morera, S. | ||||||
![]() | ![]() Title: Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Authors: Bousset, L. / Belrhali, H. / Melki, R. / Morera, S. #1: ![]() Title: Structure of the Globular Region of the Prion Protein Ure2 from the Yeast Saccharomyces cerevisiae Authors: Bousset, L. / Belrhali, H. / Janin, J. / Melki, R. / Morera, 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 | ![]() | 199.9 KB | Display | ![]() |
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PDB format | ![]() | 161 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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
#1: Protein | Mass: 29834.906 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.37 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: peg 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Details: Bousset, L., (2001) Structure, 9, 39. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 4, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. all: 57661 / Num. obs: 57630 / % possible obs: 99.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 4.9 % / Biso Wilson estimate: 34 Å2 / Rsym value: 0.071 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 2.2→2.32 Å / Redundancy: 4.7 % / Mean I/σ(I) obs: 3.2 / Num. unique all: 8292 / Rsym value: 0.221 / % possible all: 99.3 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 381950 / Rmerge(I) obs: 0.071 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 20 Å / σ(F): 2 / Rfactor obs: 0.213 | ||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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