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Open data
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Basic information
Entry | Database: PDB / ID: 8kbx | |||||||||
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Title | Cryo-EM structure of human ATG2A-WIPI4 complex | |||||||||
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![]() | LIPID TRANSPORT/MEMBRANE PROTEIN / Lipid transport / ATG2A-WIPI4 complex / single particle cryo-EM / Peripheral membrane proteins / LIPID TRANSPORT-MEMBRANE PROTEIN complex | |||||||||
Function / homology | ![]() phagophore / lipid transfer activity / organelle membrane contact site / glycophagy / phosphatidylinositol phosphate binding / nucleophagy / positive regulation of autophagosome assembly / protein localization to phagophore assembly site / phagophore assembly site membrane / piecemeal microautophagy of the nucleus ...phagophore / lipid transfer activity / organelle membrane contact site / glycophagy / phosphatidylinositol phosphate binding / nucleophagy / positive regulation of autophagosome assembly / protein localization to phagophore assembly site / phagophore assembly site membrane / piecemeal microautophagy of the nucleus / phosphatidylinositol-3-phosphate binding / phagophore assembly site / phosphatidylinositol-3,5-bisphosphate binding / reticulophagy / extrinsic component of membrane / Macroautophagy / autophagosome assembly / protein-membrane adaptor activity / cellular response to starvation / lipid droplet / autophagy / endoplasmic reticulum membrane / protein kinase binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.23 Å | |||||||||
![]() | Wang, Y. / Stjepanovic, G. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for lipid transfer by the ATG2A-ATG9A complex Authors: Wang, Y. / Stjepanovic, G. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 226.6 KB | Display | ![]() |
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PDB format | ![]() | 150.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 54 KB | Display | |
Data in CIF | ![]() | 80.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 37086MC ![]() 8kbyC ![]() 8kbzC ![]() 8kc3C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
#1: Protein | Mass: 39916.539 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 213100.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: ATG2A-WIPI4 complex / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES |
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Molecular weight | Value: 0.253 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm / C2 aperture diameter: 100 µm |
Image recording | Electron dose: 61.65 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.23 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 294088 / Symmetry type: POINT |