9jvt

Structure of the C-terminal 4 domains (V4-V6-HP) villin bound to an actin

Method: X-RAY DIFFRACTION Dmax: 141.2 Å Quality: GOOD

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 g; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Villin × 1 CA CALCIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Tris, pH 8.0 50% PEG 400 0.2 M Li2SO4 1 mM CaCl2 Resolution 3.29 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Villin × 1 CA CALCIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Tris, pH 8.0 50% PEG 400 0.2 M Li2SO4 1 mM CaCl2 Resolution 3.29 Å R-free 0.268

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 65 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 G; PDBConstruct 1–377; UniProt 1–377 Author chain g; 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 9jvt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9jvt
Deposition date deposition_date2024-10-09
Structure title titleStructure of the C-terminal 4 domains (V4-V6-HP) villin bound to an 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_guinier41.17
Radius of gyration Rg (electron density) rg_electron41.13
Forward intensity I(0) i0458149000.00
Molecular weight molecular_weight172430.0 kDa
Excluded volume excluded_volume214540 ų
Envelope volume envelope_volume291690 ų
Hydration-shell volume shell_volume60700 ų
Envelope diameter envelope_diameter147.0
Shell Rg shell_rg45.07
Envelope Rg envelope_rg40.44
Shape Rg shape_rg41.15
Total Rg total_rg41.30
Total atoms total_atoms12102
Residues n_residues1524
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 dmax141.2
Rg (real space) rg_real41.24
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real4.5810e+08
I(0) uncertainty (real space) i0_real_error9.2740e+06
Rg (reciprocal space) rg_reciprocal41.17
I(0) (reciprocal space) i0_reciprocal458100000.0000
Solution quality estimate total_estimate0.8705
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.3
Skewness Skewness skewness0.415
Kurtosis Kurtosis kurtosis-0.246
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46530000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.824

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)