[English] 日本語
Yorodumi- PDB-1rq1: Structure of Ero1p, Source of Disulfide Bonds for Oxidative Prote... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rq1 | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell | ||||||
Components | Hypothetical 65.0 kDa protein in COX14-COS3 intergenic region precursor | ||||||
Keywords | OXIDOREDUCTASE / flavoenzyme / disulfide bonds / CXXCXXC | ||||||
Function / homology | Function and homology information Insulin processing / Oxidoreductases; Acting on a sulfur group of donors; With a disulfide as acceptor / thiol oxidase activity / protein folding in endoplasmic reticulum / protein-disulfide reductase activity / FAD binding / endoplasmic reticulum membrane / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.8 Å | ||||||
Authors | Gross, E. / Kastner, D.B. / Kaiser, C.A. / Fass, D. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2004 Title: Structure of ero1p, source of disulfide bonds for oxidative protein folding in the cell. Authors: Gross, E. / Kastner, D.B. / Kaiser, C.A. / Fass, D. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1rq1.cif.gz | 84 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1rq1.ent.gz | 67.5 KB | Display | PDB format |
PDBx/mmJSON format | 1rq1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/1rq1 ftp://data.pdbj.org/pub/pdb/validation_reports/rq/1rq1 | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 44452.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: YML130C, YM4987.05C / Plasmid: pGEX-4T1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q03103 | ||||||
---|---|---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-NEN / | #4: Chemical | ChemComp-FAD / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.55 Å3/Da / Density % sol: 72.97 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: cacodylate, cadmium chloride, sodium acetate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 120 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 15, 2003 / Details: Osmic mirrors |
Radiation | Monochromator: Osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. all: 19628 / Num. obs: 19520 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 7.5 % / Biso Wilson estimate: 29.5 Å2 / Rsym value: 0.064 / Net I/σ(I): 19.2 |
-Processing
Software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MIR / Resolution: 2.8→50 Å / σ(F): 0
| |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→50 Å
| |||||||||||||||
Refine LS restraints |
|