4n78

The WAVE Regulatory Complex Links Diverse Receptors to the Actin Cytoskeleton

Method: X-RAY DIFFRACTION Dmax: 188.6 Å Quality: GOOD

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

Cytoplasmic FMR1-interacting protein 1

Homo sapiens

UniProt Q7L576

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1253 Not recorded Nck-associated protein 1 × 1 (Q9Y2A7) Wiskott-Aldrich syndrome protein family member 1 × 1 (Q92558) Protein BRICK1 × 1 (Q8WUW1) Abl interactor 2 × 1 (J3KNB2) WIRS × 1 CL CHLORIDE ION × 4 GOL GLYCEROL × 16 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;277 K;10% glycerol, 4% PEG 10,000, 12-20% PEG 300, 100 mM Tris-HCl, 2mM EDTA, 2 mM TCEP, pH 8.5, EVAPORATION, temperature 277K Resolution 2.43 Å R-free 0.209

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 CYFP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1253; UniProt 1–1253

Nck-associated protein 1

Homo sapiens

UniProt Q9Y2A7

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–1128 Not recorded Cytoplasmic FMR1-interacting protein 1 × 1 (Q7L576) Wiskott-Aldrich syndrome protein family member 1 × 1 (Q92558) Protein BRICK1 × 1 (Q8WUW1) Abl interactor 2 × 1 (J3KNB2) WIRS × 1 CL CHLORIDE ION × 4 GOL GLYCEROL × 16 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;277 K;10% glycerol, 4% PEG 10,000, 12-20% PEG 300, 100 mM Tris-HCl, 2mM EDTA, 2 mM TCEP, pH 8.5, EVAPORATION, temperature 277K Resolution 2.43 Å R-free 0.209

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 NCKP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1128; UniProt 1–1128

Wiskott-Aldrich syndrome protein family member 1

Homo sapiens

UniProt Q92558

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–559 Not recorded Cytoplasmic FMR1-interacting protein 1 × 1 (Q7L576) Nck-associated protein 1 × 1 (Q9Y2A7) Protein BRICK1 × 1 (Q8WUW1) Abl interactor 2 × 1 (J3KNB2) WIRS × 1 CL CHLORIDE ION × 4 GOL GLYCEROL × 16 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;277 K;10% glycerol, 4% PEG 10,000, 12-20% PEG 300, 100 mM Tris-HCl, 2mM EDTA, 2 mM TCEP, pH 8.5, EVAPORATION, temperature 277K Resolution 2.43 Å R-free 0.209

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 WASF1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–559; UniProt 1–559

Protein BRICK1

Homo sapiens

UniProt Q8WUW1

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–75 Not recorded Cytoplasmic FMR1-interacting protein 1 × 1 (Q7L576) Nck-associated protein 1 × 1 (Q9Y2A7) Wiskott-Aldrich syndrome protein family member 1 × 1 (Q92558) Abl interactor 2 × 1 (J3KNB2) WIRS × 1 CL CHLORIDE ION × 4 GOL GLYCEROL × 16 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;277 K;10% glycerol, 4% PEG 10,000, 12-20% PEG 300, 100 mM Tris-HCl, 2mM EDTA, 2 mM TCEP, pH 8.5, EVAPORATION, temperature 277K Resolution 2.43 Å R-free 0.209

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 BRK1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–75; UniProt 1–75

Abl interactor 2

Homo sapiens

UniProt J3KNB2

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 1–513 Not recorded Cytoplasmic FMR1-interacting protein 1 × 1 (Q7L576) Nck-associated protein 1 × 1 (Q9Y2A7) Wiskott-Aldrich syndrome protein family member 1 × 1 (Q92558) Protein BRICK1 × 1 (Q8WUW1) WIRS × 1 CL CHLORIDE ION × 4 GOL GLYCEROL × 16 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;277 K;10% glycerol, 4% PEG 10,000, 12-20% PEG 300, 100 mM Tris-HCl, 2mM EDTA, 2 mM TCEP, pH 8.5, EVAPORATION, temperature 277K Resolution 2.43 Å R-free 0.209

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 J3KNB2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 2–514; UniProt 1–513

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 4n78

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4n78
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4n78
Deposition date deposition_date2013-10-15
Structure title titleThe WAVE Regulatory Complex Links Diverse Receptors to the Actin Cytoskeleton
Keywords keywordsactin dynamics, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.51
Radius of gyration Rg (electron density) rg_electron59.48
Forward intensity I(0) i01369240000.00
Molecular weight molecular_weight313570.0 kDa
Excluded volume excluded_volume394580 ų
Envelope volume envelope_volume555460 ų
Hydration-shell volume shell_volume84829 ų
Envelope diameter envelope_diameter209.0
Shell Rg shell_rg52.44
Envelope Rg envelope_rg59.68
Shape Rg shape_rg59.49
Total Rg total_rg59.26
Total atoms total_atoms22008
Residues n_residues2702
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 dmax188.6
Rg (real space) rg_real59.34
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real1.3690e+09
I(0) uncertainty (real space) i0_real_error2.7600e+07
Rg (reciprocal space) rg_reciprocal57.79
I(0) (reciprocal space) i0_reciprocal1366000000.0000
Solution quality estimate total_estimate0.7740
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.9
Skewness Skewness skewness0.635
Kurtosis Kurtosis kurtosis-0.317
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha190500000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.740; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.806; Smooth: 0.034

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4n78D01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id4n78D02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology280 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily150
Domain ID domain_id4n78E01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id4n78F01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1620

8. Citations (1)

9. Files and Curves (10)