[English] 日本語
![](img/lk-miru.gif)
- PDB-3egx: Crystal structure of the mammalian COPII-coat protein Sec23a/24a ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 3egx | ||||||
---|---|---|---|---|---|---|---|
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 | ||||||
![]() |
| ||||||
![]() | PROTEIN TRANSPORT / COPII coat protein / vesicle transport / transport signal sequence / Disease mutation / Endoplasmic reticulum / ER-Golgi transport / Golgi apparatus / Membrane / Transport / Phosphoprotein / Transmembrane | ||||||
Function / homology | ![]() : / vesicle fusion with Golgi apparatus / Golgi trans cisterna / regulation of cholesterol transport / COPII-coated vesicle cargo loading / negative regulation of autophagosome assembly / SNARE complex / SNAP receptor activity / COPII vesicle coat / COPII vesicle coating ...: / vesicle fusion with Golgi apparatus / Golgi trans cisterna / regulation of cholesterol transport / COPII-coated vesicle cargo loading / negative regulation of autophagosome assembly / SNARE complex / SNAP receptor activity / COPII vesicle coat / COPII vesicle coating / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / COPII-mediated vesicle transport / COPI-dependent Golgi-to-ER retrograde traffic / endoplasmic reticulum exit site / endoplasmic reticulum-Golgi intermediate compartment / endoplasmic reticulum to Golgi vesicle-mediated transport / COPI-mediated anterograde transport / transport vesicle / MHC class II antigen presentation / endoplasmic reticulum-Golgi intermediate compartment membrane / GTPase activator activity / SNARE binding / protein localization to plasma membrane / cholesterol homeostasis / positive regulation of protein secretion / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / intracellular protein transport / ER to Golgi transport vesicle membrane / positive regulation of protein catabolic process / phagocytic vesicle membrane / melanosome / protein transport / ER-Phagosome pathway / Golgi membrane / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / perinuclear region of cytoplasm / zinc ion binding / membrane / cytosol 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 327.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 258.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 465.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 543 KB | Display | |
Data in XML | ![]() | 63.4 KB | Display | |
Data in CIF | ![]() | 85.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 86178.414 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#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: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50.01 % |
---|---|
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 |
---|---|
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: 1 Å / Relative weight: 1 |
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 |
-
Processing
Software |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.3→25 Å
|