8tah

Cryo-EM structure of Cortactin-bound to Arp2/3 complex

Method: ELECTRON MICROSCOPY Dmax: 144.1 Å Quality: EXCELLENT

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

Actin-related protein 3

OrganismNot specified

UniProt P61157

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–418 Not recorded Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

28 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP3_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–418; UniProt 1–418

Actin-related protein 2

OrganismNot specified

UniProt A7MB62

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–394 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–394; UniProt 1–394

Actin-related protein 2/3 complex subunit 1A

OrganismNot specified

UniProt Q1JP79

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–370 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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 ARC1A_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–370; UniProt 1–370

Actin-related protein 2/3 complex subunit 2

OrganismNot specified

UniProt Q3MHR7

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 1–300 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC2_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–300; UniProt 1–300

Actin-related protein 2/3 complex subunit 3

OrganismNot specified

UniProt Q3T035

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–178 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC3_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–178; UniProt 1–178

Actin-related protein 2/3 complex subunit 4

OrganismNot specified

UniProt Q148J6

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC4_BOVIN
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 G3MXC8

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1–151 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Src substrate cortactin × 1 (Q60598) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G3MXC8_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–151; UniProt 1–151

Src substrate cortactin

Mus musculus

UniProt Q60598

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain H; UniProt 1–76 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1A × 1 (Q1JP79) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (G3MXC8) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRC8_MOUSE
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–76; UniProt 1–76

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 8tah

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tah
Deposition date deposition_date2023-06-27
Structure title titleCryo-EM structure of Cortactin-bound to Arp2/3 complex
Keywords keywordsComplex, migration, actin, cytoskeleton, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.68
Radius of gyration Rg (electron density) rg_electron44.09
Forward intensity I(0) i0655768000.00
Molecular weight molecular_weight212710.0 kDa
Excluded volume excluded_volume266660 ų
Envelope volume envelope_volume369730 ų
Hydration-shell volume shell_volume68604 ų
Envelope diameter envelope_diameter145.7
Shell Rg shell_rg50.08
Envelope Rg envelope_rg43.53
Shape Rg shape_rg44.10
Total Rg total_rg44.34
Total atoms total_atoms14978
Residues n_residues1884
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 dmax144.1
Rg (real space) rg_real44.55
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real6.5580e+08
I(0) uncertainty (real space) i0_real_error1.1170e+07
Rg (reciprocal space) rg_reciprocal44.68
I(0) (reciprocal space) i0_reciprocal655900000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.5
Skewness Skewness skewness0.131
Kurtosis Kurtosis kurtosis-0.704
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)