[English] 日本語
![](img/lk-miru.gif)
- PDB-1g6w: CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTEIN URE... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1g6w | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTEIN URE2 FROM THE YEAST SACCAROMYCES CEREVISIAE | ||||||
![]() | URE2 PROTEIN | ||||||
![]() | STRUCTURAL GENOMICS / GST SUPERFAMILY | ||||||
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. / Janin, J. / Melki, R. / Morera, S. | ||||||
![]() | ![]() 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. #1: ![]() Title: Structural Characterization of Saccharomyces cerevisiae Prion-like Protein Ure2 Authors: Thual, C. / Komar, A.A. / Bousset, L. / Fernandez-Bellot, E. / Cullin, C. / Melki, R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 207.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 168.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 483.2 KB | Display | |
Data in XML | ![]() | 41.1 KB | Display | |
Data in CIF | ![]() | 56.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 29966.104 Da / Num. of mol.: 4 / Fragment: GLOBULAR DOMAIN (RESIDUES 94-354) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: URE2 OR YNL229C OR N1165 / Plasmid: PET3 / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 46.04 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 4000, CaCl2 , pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 50 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 14, 1999 |
Radiation | Monochromator: Asymmetric Laue C111 Diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. all: 37704 / Num. obs: 36861 / % possible obs: 95 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 3.8 % / Biso Wilson estimate: 44.454 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 5.7 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.291 / % possible all: 95 |
Reflection | *PLUS Num. measured all: 277255 |
Reflection shell | *PLUS % possible obs: 95 % / Mean I/σ(I) obs: 1.9 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
| ||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 20 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor Rwork: 0.21 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 30.41 Å2 |