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- PDB-2qtv: Structure of Sec23-Sar1 complexed with the active fragment of Sec31 -
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Open data
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Basic information
Entry | Database: PDB / ID: 2qtv | ||||||
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Title | Structure of Sec23-Sar1 complexed with the active fragment of Sec31 | ||||||
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![]() | PROTEIN TRANSPORT / COPII coat / vesicular transport / Cytoplasm / Cytoplasmic vesicle / Endoplasmic reticulum / ER-Golgi transport / Golgi apparatus / Membrane / Metal-binding / Ubl conjugation / Zinc / GTP-binding / Hydrolase / Nucleotide-binding / Phosphorylation / WD repeat | ||||||
Function / homology | ![]() Antigen Presentation: Folding, assembly and peptide loading of class I MHC / Cargo concentration in the ER / regulation of COPII vesicle coating / positive regulation of ER to Golgi vesicle-mediated transport / mitochondria-associated endoplasmic reticulum membrane contact site / COPII-mediated vesicle transport / COPII-coated vesicle budding / nuclear envelope organization / COPII-coated vesicle cargo loading / vesicle organization ...Antigen Presentation: Folding, assembly and peptide loading of class I MHC / Cargo concentration in the ER / regulation of COPII vesicle coating / positive regulation of ER to Golgi vesicle-mediated transport / mitochondria-associated endoplasmic reticulum membrane contact site / COPII-mediated vesicle transport / COPII-coated vesicle budding / nuclear envelope organization / COPII-coated vesicle cargo loading / vesicle organization / COPII vesicle coat / positive regulation of protein exit from endoplasmic reticulum / membrane organization / mating projection tip / mitochondrial fission / endoplasmic reticulum organization / mitochondrial membrane organization / reticulophagy / endoplasmic reticulum exit site / endoplasmic reticulum to Golgi vesicle-mediated transport / GTPase activator activity / macroautophagy / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / intracellular protein transport / Golgi membrane / GTPase activity / endoplasmic reticulum membrane / GTP binding / structural molecule activity / endoplasmic reticulum / mitochondrion / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Goldberg, J. / Bi, X. / Mancias, J.D. | ||||||
![]() | ![]() Title: Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Authors: Bi, X. / 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 | ![]() | 202.5 KB | Display | ![]() |
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PDB format | ![]() | 157.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 768.2 KB | Display | ![]() |
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Full document | ![]() | 794.7 KB | Display | |
Data in XML | ![]() | 38.9 KB | Display | |
Data in CIF | ![]() | 54.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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
-Protein transport protein ... , 2 types, 2 molecules AD
#1: Protein | Mass: 85735.500 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SEC23 / Production host: ![]() ![]() |
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#3: Protein/peptide | Mass: 5260.014 Da / Num. of mol.: 1 / Fragment: residues 899-947 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SEC31, WEB1 / Production host: ![]() ![]() |
-Protein , 1 types, 1 molecules B
#2: Protein | Mass: 18792.420 Da / Num. of mol.: 1 / Fragment: residues 23-189 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SAR1 / Production host: ![]() ![]() References: UniProt: P20606, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
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-Non-polymers , 4 types, 234 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/GNP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/GNP.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-ZN / |
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#5: Chemical | ChemComp-MG / |
#6: Chemical | ChemComp-GNP / |
#7: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.84 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 150 mM NaCl, 20 mM HEPES, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 10, 2004 |
Radiation | Monochromator: Pre-2007 X25 monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. all: 36685 / Num. obs: 35291 / % possible obs: 96.2 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Rmerge(I) obs: 0.078 / Χ2: 1.217 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.349 / Num. unique all: 3417 / Χ2: 1.468 / % possible all: 95 |
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Processing
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Refinement | Resolution: 2.5→30 Å / FOM work R set: 0.819 / σ(F): 718 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 29.073 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.716 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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Xplor file |
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