8uxx

Arp2/3 branch junction complex, BeFx state

Method: ELECTRON MICROSCOPY Dmax: 219.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin-related protein 3

OrganismNot specified

UniProt P32390

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–427 Not recorded Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP3_SCHPO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–427; UniProt 1–427

Actin-related protein 2

OrganismNot specified

UniProt Q9UUJ1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–390 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP2_SCHPO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–390; UniProt 1–390

Actin-related protein 2/3 complex subunit 1

OrganismNot specified

UniProt P78774

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain C; UniProt 1–377 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC1_SCHPO
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–377; UniProt 1–377

Actin-related protein 2/3 complex subunit 2

OrganismNot specified

UniProt O14241

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 1–317 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC2_SCHPO
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–317; UniProt 1–317

Actin-related protein 2/3 complex subunit 3

OrganismNot specified

UniProt Q9Y7J4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain E; UniProt 1–174 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC3_SCHPO
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–174; UniProt 1–174

Actin-related protein 2/3 complex subunit 4

OrganismNot specified

UniProt Q92352

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC4_SCHPO
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–168; UniProt 1–168

Actin-related protein 2/3 complex subunit 5

OrganismNot specified

UniProt Q10316

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain G; UniProt 1–152 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin, alpha skeletal muscle × 8 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC5_SCHPO
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–152; UniProt 1–152

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68135

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain H; UniProt 1–377 Chain I; UniProt 1–377 Chain M; UniProt 1–377 Chain N; UniProt 1–377 Chain O; UniProt 1–377 Chain P; UniProt 1–377 Chain Q; UniProt 1–377 Chain R; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) ADP ADENOSINE-5'-DIPHOSPHATE × 9 MG MAGNESIUM ION × 10 BEF BERYLLIUM TRIFLUORIDE ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The samples were incubated on the grid for 50 s and the extra solution was blotted using two Vitrobot filter papers (0.55/20 mm, Grade 595, Ted Pella) for 4 s at 0 blot force. The grids were plunged into liquid ethane at ~180 degrees C with a wait time of 0.5 s. Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–377; UniProt 1–377 Author chain I; PDBConstruct 1–377; UniProt 1–377 Author chain M; PDBConstruct 1–377; UniProt 1–377 Author chain N; PDBConstruct 1–377; UniProt 1–377 Author chain O; PDBConstruct 1–377; UniProt 1–377 Author chain P; PDBConstruct 1–377; UniProt 1–377 Author chain Q; PDBConstruct 1–377; UniProt 1–377 Author chain R; PDBConstruct 1–377; UniProt 1–377

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8uxx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uxx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uxx
Deposition date deposition_date2023-11-11
Structure title titleArp2/3 branch junction complex, BeFx state
Keywords keywordsactin, arp2/3, cytoskeleton, branch, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier62.03
Radius of gyration Rg (electron density) rg_electron62.09
Forward intensity I(0) i04399000000.00
Molecular weight molecular_weight556140.0 kDa
Excluded volume excluded_volume694480 ų
Envelope volume envelope_volume959210 ų
Hydration-shell volume shell_volume130430 ų
Envelope diameter envelope_diameter218.9
Shell Rg shell_rg61.79
Envelope Rg envelope_rg61.65
Shape Rg shape_rg62.06
Total Rg total_rg62.17
Total atoms total_atoms77507
Residues n_residues4908
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax219.4
Rg (real space) rg_real62.10
Rg uncertainty (real space) rg_real_error2.81
I(0) (real space) i0_real4.3990e+09
I(0) uncertainty (real space) i0_real_error1.1190e+08
Rg (reciprocal space) rg_reciprocal61.94
I(0) (reciprocal space) i0_reciprocal4398000000.0000
Solution quality estimate total_estimate0.8637
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.2
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha332900000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)