9jw0

Structure of the N-terminal 3 domains (V1-V3) villin bound to actin

Method: X-RAY DIFFRACTION Dmax: 97.7 Å Quality: REASONABLE

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

Actin, alpha skeletal muscle

Gallus gallus

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–377 Not recorded Villin × 1 CA CALCIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Bis-Tris propane, pH 8.5, 20% PEG 3350, 0.2 M sodium nitrate, 1 mM CaCl2 Resolution 2.69 Å R-free 0.259

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–377; UniProt 1–377

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 9jw0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jw0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jw0
Deposition date deposition_date2024-10-09
Structure title titleStructure of the N-terminal 3 domains (V1-V3) villin bound to actin
Keywords keywordsVillin Actin, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.85
Radius of gyration Rg (electron density) rg_electron29.16
Forward intensity I(0) i0105811000.00
Molecular weight molecular_weight80108.0 kDa
Excluded volume excluded_volume99785 ų
Envelope volume envelope_volume125530 ų
Hydration-shell volume shell_volume35942 ų
Envelope diameter envelope_diameter107.3
Shell Rg shell_rg36.33
Envelope Rg envelope_rg29.06
Shape Rg shape_rg29.15
Total Rg total_rg29.85
Total atoms total_atoms5620
Residues n_residues706
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 dmax97.7
Rg (real space) rg_real29.77
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.0580e+08
I(0) uncertainty (real space) i0_real_error1.6900e+06
Rg (reciprocal space) rg_reciprocal29.81
I(0) (reciprocal space) i0_reciprocal105800000.0000
Solution quality estimate total_estimate0.7016
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.9
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.520
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22410000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 0.135; Positv: 1.000; Valcen: 0.997; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)