9i2b

SPIN90-Arp2/3 nucleated bidirectional actin filaments

Method: ELECTRON MICROSCOPY Dmax: 224.0 Å Quality: GOOD

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

Actin-related protein 2

Homo sapiens

UniProt P61160

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 L; UniProt 1–394 Not recorded Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–394; UniProt 1–394 Author chain L; PDBConstruct 1–394; UniProt 1–394

Actin-related protein 2/3 complex subunit 2

Homo sapiens

UniProt O15144

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 N; UniProt 1–300 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 ARPC2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–300; UniProt 1–300 Author chain N; PDBConstruct 1–300; UniProt 1–300

Actin-related protein 2/3 complex subunit 3

Homo sapiens

UniProt O15145

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 O; UniProt 1–178 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 ARPC3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–178; UniProt 1–178 Author chain O; PDBConstruct 1–178; UniProt 1–178

Actin-related protein 2/3 complex subunit 4

Homo sapiens

UniProt P59998

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 P; UniProt 1–168 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 ARPC4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–168; UniProt 1–168 Author chain P; PDBConstruct 1–168; UniProt 1–168

Actin-related protein 2/3 complex subunit 5-like protein

Homo sapiens

UniProt Q9BPX5

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 1–153 Chain Q; UniProt 1–153 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP5L_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–153; UniProt 1–153 Author chain Q; PDBConstruct 1–153; UniProt 1–153

Actin, cytoplasmic 1

OrganismNot specified

UniProt Q6QAQ1

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 1–375 Chain J; UniProt 1–375 Chain S; UniProt 1–375 Chain T; UniProt 1–375 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_PIG
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–375; UniProt 1–375 Author chain J; PDBConstruct 1–375; UniProt 1–375 Author chain S; PDBConstruct 1–375; UniProt 1–375 Author chain T; PDBConstruct 1–375; UniProt 1–375

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 1–722 Chain R; UniProt 1–722 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 Actin-related protein 2/3 complex subunit 1B × 2 (O15143) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1–722; UniProt 1–722 Author chain R; PDBConstruct 1–722; UniProt 1–722

Actin-related protein 2/3 complex subunit 1B

Homo sapiens

UniProt O15143

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 M; UniProt 1–372 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 3 × 2 (P61158) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARC1B_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain C; PDBConstruct 1–372; UniProt 1–372 Author chain M; PDBConstruct 1–372; UniProt 1–372

Actin-related protein 3

Homo sapiens

UniProt P61158

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 K; UniProt 1–418 Not recorded Actin-related protein 2 × 2 (P61160) Actin-related protein 2/3 complex subunit 2 × 2 (O15144) Actin-related protein 2/3 complex subunit 3 × 2 (O15145) Actin-related protein 2/3 complex subunit 4 × 2 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 2 (Q9BPX5) Actin, cytoplasmic 1 × 4 (Q6QAQ1) Phalloidin × 4 NCK-interacting protein with SH3 domain × 2 (Q9NZQ3) Actin-related protein 2/3 complex subunit 1B × 2 (O15143) ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 ARP3_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain A; PDBConstruct 1–418; UniProt 1–418 Author chain K; PDBConstruct 1–418; UniProt 1–418

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 9i2b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i2b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i2b
Deposition date deposition_date2025-01-20
Structure title titleSPIN90-Arp2/3 nucleated bidirectional actin filaments
Keywords keywordsCytoskeleton, Branched actin network, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.67
Radius of gyration Rg (electron density) rg_electron75.22
Forward intensity I(0) i06681600000.00
Molecular weight molecular_weight695650.0 kDa
Excluded volume excluded_volume871880 ų
Envelope volume envelope_volume1302700 ų
Hydration-shell volume shell_volume153270 ų
Envelope diameter envelope_diameter295.2
Shell Rg shell_rg68.83
Envelope Rg envelope_rg73.56
Shape Rg shape_rg75.20
Total Rg total_rg75.19
Total atoms total_atoms97342
Residues n_residues6144
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 dmax224.0
Rg (real space) rg_real72.55
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real6.5820e+09
I(0) uncertainty (real space) i0_real_error1.2670e+08
Rg (reciprocal space) rg_reciprocal72.59
I(0) (reciprocal space) i0_reciprocal6646000000.0000
Solution quality estimate total_estimate0.8326
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary74.7
Skewness Skewness skewness0.510
Kurtosis Kurtosis kurtosis-0.292
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0508
Highest regularization parameter α highest_alpha331100000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.891; Stabil: 0.990; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.038

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)