9dlz

Bovine Arp2/3 complex with N-WASP CA bound to Arp3

Method: ELECTRON MICROSCOPY Dmax: 146.3 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 3–413 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–411; UniProt 3–413

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–390 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–390; UniProt 1–390

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 × 9 PDB declaration: nonameric(9) 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 1–285 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–285; UniProt 1–285

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain E; UniProt 2–176 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–175; UniProt 2–176

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain F; UniProt 2–168 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–167; UniProt 2–168

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 7–151 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) WASP like actin nucleation promoting factor × 2 (A0A7J7WN29) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–145; UniProt 7–151

WASP like actin nucleation promoting factor

Homo sapiens

UniProt A0A7J7WN29

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 500–540 Chain I; UniProt 500–540 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 A0A7J7WN29_PIPKU
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–41; UniProt 500–540 Author chain I; PDBConstruct 1–41; UniProt 500–540

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 9dlz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dlz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9dlz
Deposition date deposition_date2024-09-11
Structure title titleBovine Arp2/3 complex with N-WASP CA bound to Arp3
Keywords keywordsactin, arp 2-3 complex, N-WASP, nucleation promoting factor, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.86
Radius of gyration Rg (electron density) rg_electron45.25
Forward intensity I(0) i0700820000.00
Molecular weight molecular_weight219650.0 kDa
Excluded volume excluded_volume275290 ų
Envelope volume envelope_volume396420 ų
Hydration-shell volume shell_volume72006 ų
Envelope diameter envelope_diameter145.7
Shell Rg shell_rg50.73
Envelope Rg envelope_rg44.46
Shape Rg shape_rg45.25
Total Rg total_rg45.48
Total atoms total_atoms15455
Residues n_residues1927
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 dmax146.3
Rg (real space) rg_real45.69
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real7.0080e+08
I(0) uncertainty (real space) i0_real_error1.2040e+07
Rg (reciprocal space) rg_reciprocal45.86
I(0) (reciprocal space) i0_reciprocal701000000.0000
Solution quality estimate total_estimate0.9022
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.0
Skewness Skewness skewness0.122
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha110900000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.894

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)