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- PDB-1rp4: Structure of Ero1p, Source of Disulfide Bonds for Oxidative Prote... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rp4 | ||||||
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Title | Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell | ||||||
![]() | Hypothetical 65.0 kDa protein in COX14-COS3 intergenic region precursor | ||||||
![]() | OXIDOREDUCTASE / flavoenzyme / disulfide bonds / CXXCXXC | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gross, E. / Kastner, D.B. / Kaiser, C.A. / Fass, D. | ||||||
![]() | ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 89 KB | Display | ![]() |
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PDB format | ![]() | 71.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 877.4 KB | Display | ![]() |
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Full document | ![]() | 895.3 KB | Display | |
Data in XML | ![]() | 19.3 KB | Display | |
Data in CIF | ![]() | 25.9 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: 45179.746 Da / Num. of mol.: 1 / Fragment: Ero1p-c Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: YML130C, YM4987.05C / Plasmid: pGEX-4T1 / Production host: ![]() ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-NEN / | #4: Chemical | ChemComp-FAD / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.12 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: sodium acetate, cacodylate, cadmium sulfate, ethanol, methanol , pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 20K |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Mar 20, 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: 2.2→50 Å / Num. all: 26194 / Num. obs: 25802 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Redundancy: 6.8 % / Biso Wilson estimate: 29.5 Å2 / Rsym value: 0.067 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 3.5 / Num. unique all: 2556 / Rsym value: 0.554 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.2→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.28 Å
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