9m64

Structure of SPIN90 dimer-Arp2/3 complexes-nucleated actin filaments (Doublet Complex)

Method: ELECTRON MICROSCOPY Dmax: 252.7 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 1–418 Chain a; UniProt 1–418 Not recorded Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1–418; UniProt 1–418 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain B; UniProt 1–394 Chain b; UniProt 1–394 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1–394; UniProt 1–394 Author chain b; PDBConstruct 1–394; UniProt 1–394

Actin-related protein 2/3 complex subunit 1B

OrganismNot specified

UniProt Q58CQ2

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain C; UniProt 1–372 Chain c; UniProt 1–372 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARC1B_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–372; UniProt 1–372 Author chain c; PDBConstruct 1–372; UniProt 1–372

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain D; UniProt 1–300 Chain d; UniProt 1–300 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1–300; UniProt 1–300 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain E; UniProt 1–178 Chain e; UniProt 1–178 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1–178; UniProt 1–178 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain F; UniProt 1–168 Chain f; UniProt 1–168 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1–168; UniProt 1–168 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain G; UniProt 1–151 Chain g; UniProt 1–151 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1–151; UniProt 1–151 Author chain g; PDBConstruct 1–151; UniProt 1–151

NCK-interacting protein with SH3 domain

Homo sapiens

UniProt Q9NZQ3

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain H; UniProt 269–722 Chain h; UniProt 269–722 Not recorded Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPN90_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–454; UniProt 269–722 Author chain h; PDBConstruct 1–454; UniProt 269–722

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68139

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain I; UniProt 1–377 Chain J; UniProt 1–377 Chain K; UniProt 1–377 Chain L; UniProt 1–377 Chain i; UniProt 1–377 Chain j; UniProt 1–377 Chain k; UniProt 1–377 Chain l; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-related protein 3 × 2 (P61157) Actin-related protein 2 × 2 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 2 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 2 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 2 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 2 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 2 (Q3SYX9) NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

57 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–377; UniProt 1–377 Author chain J; PDBConstruct 1–377; UniProt 1–377 Author chain K; PDBConstruct 1–377; UniProt 1–377 Author chain L; PDBConstruct 1–377; UniProt 1–377 Author chain i; PDBConstruct 1–377; UniProt 1–377 Author chain j; PDBConstruct 1–377; UniProt 1–377 Author chain k; PDBConstruct 1–377; UniProt 1–377 Author chain l; 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 9m64

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m64
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m64
Deposition date deposition_date2025-03-07
Structure title titleStructure of SPIN90 dimer-Arp2/3 complexes-nucleated actin filaments (Doublet Complex)
Keywords keywordsSPIN90, actin, cytoskeleton, Arp2-3 complex, Nucleation Promoting Factor, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier94.33
Radius of gyration Rg (electron density) rg_electron95.72
Forward intensity I(0) i09365750000.00
Molecular weight molecular_weight812750.0 kDa
Excluded volume excluded_volume1012900 ų
Envelope volume envelope_volume1650400 ų
Hydration-shell volume shell_volume165910 ų
Envelope diameter envelope_diameter407.1
Shell Rg shell_rg71.68
Envelope Rg envelope_rg98.72
Shape Rg shape_rg95.90
Total Rg total_rg94.79
Total atoms total_atoms57141
Residues n_residues7493
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 dmax252.7
Rg (real space) rg_real85.91
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real8.8860e+09
I(0) uncertainty (real space) i0_real_error1.7140e+08
Rg (reciprocal space) rg_reciprocal85.68
I(0) (reciprocal space) i0_reciprocal9121000000.0000
Solution quality estimate total_estimate0.9132
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.0
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.5495
Highest regularization parameter α highest_alpha335300000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.022; Oscil: 0.961; Stabil: 0.987; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.039

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)