7usc

Cryo-EM structure of WAVE Regulatory Complex

Method: ELECTRON MICROSCOPY Dmax: 189.7 Å Quality: REASONABLE

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 × 5 PDB declaration: pentameric(5) 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 (E9PEZ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 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 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 × 5 PDB declaration: pentameric(5) 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 (E9PEZ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 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 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–230 Chain C; UniProt 485–559 Not recorded Cytoplasmic FMR1-interacting protein 1 × 1 (Q7L576) Nck-associated protein 1 × 1 (Q9Y2A7) Protein BRICK1 × 1 (Q8WUW1) Abl interactor 2 × 1 (E9PEZ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 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 WASF1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–230; UniProt 1–230 Author chain C; PDBConstruct 249–323; UniProt 485–559

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; 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 (E9PEZ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 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 BRK1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–75; UniProt 1–75

Abl interactor 2

Homo sapiens

UniProt E9PEZ7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–158 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 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 E9PEZ7_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–158; UniProt 1–158

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 7usc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7usc
Deposition date deposition_date2022-04-25
Structure title titleCryo-EM structure of WAVE Regulatory Complex
Keywords keywordsactin regulator, GTPase binding protein, cytoskeletal regulator, CELL INVASION; CELL INVASION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.87
Radius of gyration Rg (electron density) rg_electron59.77
Forward intensity I(0) i01333860000.00
Molecular weight molecular_weight309120.0 kDa
Excluded volume excluded_volume388910 ų
Envelope volume envelope_volume549980 ų
Hydration-shell volume shell_volume84377 ų
Envelope diameter envelope_diameter209.7
Shell Rg shell_rg52.02
Envelope Rg envelope_rg59.66
Shape Rg shape_rg59.77
Total Rg total_rg59.55
Total atoms total_atoms21709
Residues n_residues2673
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 dmax189.7
Rg (real space) rg_real59.71
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real1.3340e+09
I(0) uncertainty (real space) i0_real_error2.5440e+07
Rg (reciprocal space) rg_reciprocal58.12
I(0) (reciprocal space) i0_reciprocal1331000000.0000
Solution quality estimate total_estimate0.5456
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.2
Skewness Skewness skewness0.635
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha196200000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 0.009; Positv: 1.000; Valcen: 0.805; Smooth: 0.044

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)