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Open data
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Basic information
Entry | Database: PDB / ID: 1k8k | ||||||
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Title | Crystal Structure of Arp2/3 Complex | ||||||
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![]() | STRUCTURAL PROTEIN / beta-propeller | ||||||
Function / homology | ![]() 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 ...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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Robinson, R.C. / Turbedsky, K. / Kaiser, D.A. / Higgs, H.N. / Marchand, J.-B. / Choe, S. / Pollard, T.D. | ||||||
![]() | ![]() Title: Crystal Structure of Arp2/3 Complex Authors: Robinson, R.C. / Turbedsky, K. / Kaiser, D.A. / Marchand, J.-B. / Higgs, H.N. / Choe, S. / Pollard, T.D. #1: ![]() Title: Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization Authors: Higgs, H.N. / Blanchoin, L. / Pollard, T.D. #2: ![]() Title: Structure and function of the Arp2/3 complex Authors: Mullins, R.D. / Pollard, T.D. #3: ![]() Title: Biophysics of actin filament dynamics in nonmuscle cells Authors: Pollard, T.D. / Blanchoin, L. / Mullins, R.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 393.9 KB | Display | ![]() |
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PDB format | ![]() | 311.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.7 KB | Display | ![]() |
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Full document | ![]() | 527.3 KB | Display | |
Data in XML | ![]() | 84.1 KB | Display | |
Data in CIF | ![]() | 122.6 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
-ACTIN-LIKE PROTEIN ... , 2 types, 2 molecules AB
#1: Protein | Mass: 47428.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 44818.711 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
-ARP2/3 COMPLEX ... , 5 types, 5 molecules CDEFG
#3: Protein | Mass: 41016.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
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#4: Protein | Mass: 34402.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
#5: Protein | Mass: 20572.666 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
#6: Protein | Mass: 19697.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
#7: Protein | Mass: 16295.317 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: part of the Arp2/3 Complex / Source: (natural) ![]() ![]() |
-Non-polymers , 1 types, 1710 molecules 
#8: Water | ChemComp-HOH / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.33 Å3/Da / Density % sol: 63.03 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 25, 2001 / Details: double crystal monochromator |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2→40 Å / Num. all: 196866 / Num. obs: 185141 / % possible obs: 92 % / Observed criterion σ(I): 1 / Redundancy: 4.6 % / Biso Wilson estimate: 39.5 Å2 / Rmerge(I) obs: 0.071 / Rsym value: 0.064 / Net I/σ(I): 8.6 |
Reflection | *PLUS Highest resolution: 2.01 Å / Lowest resolution: 20 Å / Num. obs: 183319 / % possible obs: 92.8 % / Num. measured all: 852046 / Rmerge(I) obs: 0.064 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.01 Å / Lowest resolution: 20 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.216 / Rfactor Rfree: 0.249 | ||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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