8e9b

Cryo-EM structure of S. pombe Arp2/3 complex in the branch junction

Method: ELECTRON MICROSCOPY Dmax: 246.8 Å Quality: GOOD

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

Actin-related protein 3

OrganismNot specified

UniProt P32390

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–427 Not recorded Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP3_SCHPO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–427; UniProt 1–427

Actin-related protein 2

OrganismNot specified

UniProt Q9UUJ1

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–390 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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_SCHPO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–390; UniProt 1–390

Actin-related protein 2/3 complex subunit 1

OrganismNot specified

UniProt P78774

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain C; UniProt 1–377 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC1_SCHPO
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–377; UniProt 1–377

Actin-related protein 2/3 complex subunit 2

OrganismNot specified

UniProt O14241

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 1–317 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC2_SCHPO
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–317; UniProt 1–317

Actin-related protein 2/3 complex subunit 3

OrganismNot specified

UniProt Q9Y7J4

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain E; UniProt 1–174 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC3_SCHPO
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–174; UniProt 1–174

Actin-related protein 2/3 complex subunit 4

OrganismNot specified

UniProt Q92352

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC4_SCHPO
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 Q10316

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain G; UniProt 1–152 Not recorded Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin, alpha skeletal muscle × 8 (P68139) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC5_SCHPO
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–152; UniProt 1–152

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain H; UniProt 3–377 Chain I; UniProt 3–377 Chain M; UniProt 3–377 Chain N; UniProt 3–377 Chain O; UniProt 3–377 Chain P; UniProt 3–377 Chain Q; UniProt 3–377 Chain R; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-related protein 3 × 1 (P32390) Actin-related protein 2 × 1 (Q9UUJ1) Actin-related protein 2/3 complex subunit 1 × 1 (P78774) Actin-related protein 2/3 complex subunit 2 × 1 (O14241) Actin-related protein 2/3 complex subunit 3 × 1 (Q9Y7J4) Actin-related protein 2/3 complex subunit 4 × 1 (Q92352) Actin-related protein 2/3 complex subunit 5 × 1 (Q10316) MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 8
Chains and sequence ranges Author chain H; PDBConstruct 1–375; UniProt 3–377 Author chain I; PDBConstruct 1–375; UniProt 3–377 Author chain M; PDBConstruct 1–375; UniProt 3–377 Author chain N; PDBConstruct 1–375; UniProt 3–377 Author chain O; PDBConstruct 1–375; UniProt 3–377 Author chain P; PDBConstruct 1–375; UniProt 3–377 Author chain Q; PDBConstruct 1–375; UniProt 3–377 Author chain R; PDBConstruct 1–375; UniProt 3–377

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 8e9b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e9b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e9b
Deposition date deposition_date2022-08-26
最后修订 last_revision2023-02-01
Structure title titleCryo-EM structure of S. pombe Arp2/3 complex in the branch junction
Keywords keywordsArp2-3 complex, branch juction, polymerization, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.06
Radius of gyration Rg (electron density) rg_electron63.13
Forward intensity I(0) i04421470000.00
Molecular weight molecular_weight557550.0 kDa
Excluded volume excluded_volume696250 ų
Envelope volume envelope_volume984600 ų
Hydration-shell volume shell_volume132340 ų
Envelope diameter envelope_diameter219.0
Shell Rg shell_rg62.48
Envelope Rg envelope_rg62.35
Shape Rg shape_rg63.10
Total Rg total_rg63.21
Total atoms total_atoms39160
Residues n_residues4925
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 dmax246.8
Rg (real space) rg_real67.62
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real4.4780e+09
I(0) uncertainty (real space) i0_real_error9.7080e+07
Rg (reciprocal space) rg_reciprocal62.96
I(0) (reciprocal space) i0_reciprocal4420000000.0000
Solution quality estimate total_estimate0.8671
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.1
Skewness Skewness skewness0.663
Kurtosis Kurtosis kurtosis0.301
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.8615
Highest regularization parameter α highest_alpha380700000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.676; Stabil: 0.823; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.834

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id8e9bA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8e9bB01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8e9bC01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8e9bD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id8e9bG01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily190 — Actin-related protein 2/3 complex subunit 5

8. Citations (1)

9. Files and Curves (10)