7jpn

Cryo-EM structure of Arpin-bound Arp2/3 complex

Method: ELECTRON MICROSCOPY Dmax: 135.2 Å Quality: REASONABLE

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 3–415 Not recorded Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) 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 (G3MXC8) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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 1–413; UniProt 3–415

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 4–380 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) 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 (G3MXC8) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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 1–377; UniProt 4–380

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–372 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 (G3MXC8) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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

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 1B × 1 (Q58CQ2) 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 (G3MXC8) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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 1B × 1 (Q58CQ2) 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 (G3MXC8) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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 1B × 1 (Q58CQ2) 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 (G3MXC8) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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 G3MXC8

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 9–151 Not recorded Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) 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) Arpin × 1 (Q7Z6K5) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G3MXC8_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–143; UniProt 9–151

Arpin

Homo sapiens

UniProt Q7Z6K5

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 193–226 Fragment:UNP residues 193-226 Actin-related protein 3 × 1 (P61157) Actin-related protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) 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 (G3MXC8) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were manually blotted for 3 seconds with Whatman 41 filter paper and manually plunged using a Leica EM CPC manual plunger. Resolution 3.24 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 ARPIN_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–34; UniProt 193–226

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 7jpn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7jpn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7jpn
Deposition date deposition_date2020-08-09
Structure title titleCryo-EM structure of Arpin-bound Arp2/3 complex
Keywords keywords;actin, ATPase, actin related protein, arp, cytoskeleton, Arp2-3 complex, actin nucleation, actin branching, CONTRACTILE PROTEIN, Arpin ;; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.87
Radius of gyration Rg (electron density) rg_electron43.31
Forward intensity I(0) i0663203000.00
Molecular weight molecular_weight213730.0 kDa
Excluded volume excluded_volume267850 ų
Envelope volume envelope_volume355890 ų
Hydration-shell volume shell_volume66965 ų
Envelope diameter envelope_diameter144.4
Shell Rg shell_rg49.54
Envelope Rg envelope_rg42.99
Shape Rg shape_rg43.31
Total Rg total_rg43.57
Total atoms total_atoms15040
Residues n_residues1885
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 dmax135.2
Rg (real space) rg_real44.57
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real6.5210e+08
I(0) uncertainty (real space) i0_real_error9.2910e+06
Rg (reciprocal space) rg_reciprocal43.87
I(0) (reciprocal space) i0_reciprocal663300000.0000
Solution quality estimate total_estimate0.7109
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.3
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.597
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha2.2730
Highest regularization parameter α highest_alpha104600000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 0.911; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.584

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7jpnA01
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_id7jpnC01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)