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Open data
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Basic information
| Entry | Database: PDB / ID: 2p9s | ||||||
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| Title | Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+ | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / actin / WD repeat / complex | ||||||
| Function / homology | Function and homology informationmuscle cell projection membrane / 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 / regulation of actin filament polymerization / Clathrin-mediated endocytosis / Neutrophil degranulation / positive regulation of actin filament polymerization ...muscle cell projection membrane / 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 / regulation of actin filament polymerization / Clathrin-mediated endocytosis / Neutrophil degranulation / positive regulation of actin filament polymerization / cilium assembly / positive regulation of double-strand break repair via homologous recombination / positive regulation of lamellipodium assembly / actin filament polymerization / positive regulation of substrate adhesion-dependent cell spreading / cell projection / structural constituent of cytoskeleton / actin filament binding / synaptic vesicle membrane / cell migration / lamellipodium / site of double-strand break / actin binding / cell cortex / postsynapse / neuron projection / endosome / focal adhesion / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.68 Å | ||||||
Authors | Nolen, B.J. / Pollard, T.D. | ||||||
Citation | Journal: Mol.Cell / Year: 2007Title: Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex. Authors: Nolen, B.J. / Pollard, T.D. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2p9s.cif.gz | 355.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2p9s.ent.gz | 278.6 KB | Display | PDB format |
| PDBx/mmJSON format | 2p9s.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p9/2p9s ftp://data.pdbj.org/pub/pdb/validation_reports/p9/2p9s | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 2p9iC ![]() 2p9kC ![]() 2p9lC ![]() 2p9nC ![]() 2p9pC ![]() 2p9uC C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
-Actin-like protein ... , 2 types, 2 molecules AB
| #1: Protein | Mass: 47428.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #2: Protein | Mass: 44818.711 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
-Actin-related protein 2/3 complex subunit ... , 5 types, 5 molecules CDEFG
| #3: Protein | Mass: 41016.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #4: Protein | Mass: 34402.043 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
| #5: Protein | Mass: 20572.666 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
| #6: Protein | Mass: 19697.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
| #7: Protein | Mass: 16295.317 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
-Non-polymers , 3 types, 236 molecules 




| #8: Chemical | ChemComp-MG / | ||
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| #9: Chemical | | #10: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 61.65 % |
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.9795 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 18, 2005 |
| Radiation | Monochromator: Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
| Reflection | Resolution: 2.68→30 Å / Num. all: 81381 / Num. obs: 80893 / % possible obs: 0.994 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Rsym value: 10.4 / Net I/σ(I): 22.3 |
| Reflection shell | Resolution: 2.68→2.78 Å / Mean I/σ(I) obs: 2.6 / Rsym value: 0.544 / % possible all: 0.961 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.68→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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| Solvent computation | Bsol: 30.013 Å2 | ||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 52.779 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.68→30 Å
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| Refine LS restraints |
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| Xplor file |
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X-RAY DIFFRACTION
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