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Open data
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Basic information
Entry | Database: PDB / ID: 3m31 | ||||||
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Title | Structure of the C150A/C295A mutant of S. cerevisiae Ero1p | ||||||
![]() | Endoplasmic oxidoreductin-1 | ||||||
![]() | OXIDOREDUCTASE / disulfide mutant / Disulfide bond / Electron transport / Endoplasmic reticulum / FAD / Flavoprotein / Glycoprotein / Membrane / Redox-active center / Transport | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Heldman, N. / Fass, D. | ||||||
![]() | ![]() Title: Steps in reductive activation of the disulfide-generating enzyme Ero1p Authors: Heldman, N. / Vonshak, O. / Sevier, C.S. / Vitu, E. / Mehlman, T. / 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 | ![]() | 95.1 KB | Display | ![]() |
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PDB format | ![]() | 70.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 877.2 KB | Display | ![]() |
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Full document | ![]() | 888.6 KB | Display | |
Data in XML | ![]() | 18.9 KB | Display | |
Data in CIF | ![]() | 26.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3nvjC ![]() 1rp4S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 44730.305 Da / Num. of mol.: 1 / Fragment: residues in UNP 56-424 / Mutation: C150A, C295A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: ERO1 / Plasmid: modified pGEX-4T1 / Production host: ![]() ![]() References: UniProt: Q03103, Oxidoreductases; Acting on a sulfur group of donors; With a disulfide as acceptor |
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#2: Chemical | ChemComp-NEN / |
#3: Chemical | ChemComp-FAD / |
#4: Chemical | ChemComp-CD / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.04 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: 100mM cacodylic acid, 10mM cadmium sulfate, 2% methanol, 2% ethanol, 1.2M sodium acetate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.85→50 Å / Num. all: 43123 / Num. obs: 42677 / % possible obs: 99 % / Redundancy: 4.9 % / Rsym value: 0.037 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 2.2 / Num. unique all: 4231 / Rsym value: 0.521 / % possible all: 92.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1RP4 after removal of residues 146 to 166 and 291 to 302 Resolution: 1.85→50 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.85→50 Å
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Refine LS restraints |
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