9eam

Coronin-7 CA bound to Arp2/3 complex

Method: ELECTRON MICROSCOPY Dmax: 146.8 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 (Q3SYX9) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 (Q3SYX9) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 (Q3SYX9) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 (Q3SYX9) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 (Q3SYX9) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 (Q3SYX9) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 Q3SYX9

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) Coronin-7 × 1 (P57737) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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.

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

View Construct and Data Evidence
UniProt name ARPC5_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–151; UniProt 1–151

Coronin-7

Homo sapiens

UniProt P57737

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 888–925 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 (Q3SYX9) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name CORO7_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–38; UniProt 888–925

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 9eam

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9eam
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9eam
Deposition date deposition_date2024-11-11
Structure title titleCoronin-7 CA bound to Arp2/3 complex
Keywords keywordscytoskeleton, actin, cell motility, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.29
Radius of gyration Rg (electron density) rg_electron45.69
Forward intensity I(0) i0733967000.00
Molecular weight molecular_weight224300.0 kDa
Excluded volume excluded_volume280920 ų
Envelope volume envelope_volume413880 ų
Hydration-shell volume shell_volume74393 ų
Envelope diameter envelope_diameter148.3
Shell Rg shell_rg51.38
Envelope Rg envelope_rg44.69
Shape Rg shape_rg45.69
Total Rg total_rg45.95
Total atoms total_atoms15778
Residues n_residues1967
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 dmax146.8
Rg (real space) rg_real46.11
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real7.3400e+08
I(0) uncertainty (real space) i0_real_error1.2000e+07
Rg (reciprocal space) rg_reciprocal46.29
I(0) (reciprocal space) i0_reciprocal734100000.0000
Solution quality estimate total_estimate0.9019
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.1
Skewness Skewness skewness0.116
Kurtosis Kurtosis kurtosis-0.690
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha126400000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)