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- PDB-3egx: Crystal structure of the mammalian COPII-coat protein Sec23a/24a ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3egx | ||||||
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Title | Crystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22b and bound to the transport signal sequence of the SNARE protein Bet1 | ||||||
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Function / homology | ![]() vesicle fusion with Golgi apparatus / Golgi trans cisterna / regulation of cholesterol transport / COPII vesicle coating / COPII-coated vesicle cargo loading / integral component of Golgi membrane / COPII vesicle coat / negative regulation of autophagosome assembly / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Goldberg, J. / Mancias, J.D. | ||||||
![]() | ![]() Title: Structural basis of cargo membrane protein discrimination by the human COPII coat machinery. Authors: Mancias, J.D. / Goldberg, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 322.3 KB | Display | ![]() |
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PDB format | ![]() | 262.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 328.3 KB | Display | ![]() |
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Full document | ![]() | 405.5 KB | Display | |
Data in XML | ![]() | 67.1 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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Unit cell |
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Components
#1: Protein | ![]() Mass: 86178.414 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Protein | ![]() Mass: 84336.820 Da / Num. of mol.: 1 / Fragment: Conserved core, UNP residues 346-1093 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
#3: Protein | Mass: 18031.645 Da / Num. of mol.: 1 / Fragment: cytoplasmic domainn, UNP residues 1-157 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
#4: Protein/peptide | Mass: 1000.984 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic 9-residue peptide / References: UniProt: O15155*PLUS |
#5: Chemical |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50.01 % |
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Crystal grow![]() | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.9 Details: 10% (w/v) PEG 4000, 0.1 M NaCl, 0.5 M sodium acetate, 50 mM Tris buffer, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 5, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.3→25 Å / Num. obs: 24079 / % possible obs: 92 % / Observed criterion σ(F): 1 / Redundancy: 2.7 % / Rmerge(I) obs: 0.111 / Net I/σ(I): 9.6 |
Reflection shell | Resolution: 3.3→3.4 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.394 / Mean I/σ(I) obs: 2.2 / % possible all: 95.1 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Refinement step | Cycle: LAST / Resolution: 3.3→25 Å
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