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- PDB-9dlx: Bovine Arp2/3 complex with N-WASP CA bound to Arp3 and Arp2-ArpC1 -
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Open data
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Basic information
Entry | Database: PDB / ID: 9dlx | ||||||
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Title | Bovine Arp2/3 complex with N-WASP CA bound to Arp3 and Arp2-ArpC1 | ||||||
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![]() | STRUCTURAL PROTEIN / actin / arp 2-3 complex / N-WASP / nucleation promoting factor | ||||||
Function / homology | ![]() negative regulation of membrane tubulation / muscle cell projection membrane / spindle localization / positive regulation of clathrin-dependent endocytosis / EPHB-mediated forward signaling / Regulation of actin dynamics for phagocytic cup formation / RHO GTPases Activate WASPs and WAVEs / Arp2/3 protein complex / Arp2/3 complex-mediated actin nucleation / negative regulation of lymphocyte migration ...negative regulation of membrane tubulation / muscle cell projection membrane / spindle localization / positive regulation of clathrin-dependent endocytosis / EPHB-mediated forward signaling / Regulation of actin dynamics for phagocytic cup formation / RHO GTPases Activate WASPs and WAVEs / Arp2/3 protein complex / Arp2/3 complex-mediated actin nucleation / negative regulation of lymphocyte migration / vesicle transport along actin filament / GTPase regulator activity / NOSTRIN mediated eNOS trafficking / actin cap / vesicle organization / regulation of actin filament polymerization / vesicle budding from membrane / Clathrin-mediated endocytosis / dendritic spine morphogenesis / actin polymerization or depolymerization / protein-containing complex localization / Nephrin family interactions / DCC mediated attractive signaling / regulation of postsynapse organization / positive regulation of filopodium assembly / Neutrophil degranulation / RHOV GTPase cycle / RHOJ GTPase cycle / RHOQ GTPase cycle / CDC42 GTPase cycle / cilium assembly / RHO GTPases Activate WASPs and WAVEs / positive regulation of double-strand break repair via homologous recombination / positive regulation of lamellipodium assembly / actin filament polymerization / EPHB-mediated forward signaling / RAC1 GTPase cycle / cell projection / FCGR3A-mediated phagocytosis / response to bacterium / Regulation of actin dynamics for phagocytic cup formation / structural constituent of cytoskeleton / actin filament binding / endocytic vesicle membrane / cell migration / lamellipodium / actin cytoskeleton / regulation of protein localization / Clathrin-mediated endocytosis / site of double-strand break / actin binding / actin cytoskeleton organization / cell cortex / protein-containing complex assembly / cytoplasmic vesicle / neuron projection / cell division / synapse / endoplasmic reticulum membrane / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / extracellular exosome / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.91 Å | ||||||
![]() | Saks, A.J. / Barrie, K.R. / Dominguez, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Arp 2/3 complex with bound NPFs Authors: Saks, A.J. / Barrie, K.R. / Dominguez, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 399.7 KB | Display | ![]() |
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PDB format | ![]() | 317.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 46992MC ![]() 9dlzC C: citing same article ( M: map data used to model this data |
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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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Components
-Actin-related protein ... , 7 types, 7 molecules ABCDEFG
#1: Protein | Mass: 46851.305 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 44362.152 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 41594.238 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#4: Protein | Mass: 32672.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#5: Protein | Mass: 20256.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#6: Protein | Mass: 19565.852 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#7: Protein | Mass: 16251.308 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein/peptide , 1 types, 2 molecules HI
#8: Protein/peptide | Mass: 4750.827 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 2 types, 4 molecules 


#9: Chemical | #10: Chemical | |
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-Details
Has ligand of interest | N |
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Has protein modification | N |
-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: Arp 2/3 complex bound to NPFs / Type: COMPLEX / Entity ID: #3-#8 / Source: NATURAL |
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Molecular weight | Value: 0.22 MDa / Experimental value: YES |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
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: OTHER / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 47 e/Å2 / Film or detector model: OTHER |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 292065 / Symmetry type: POINT |