9sr0

Mouse vinculin head domain 1 (VD1) (residues 2-258) with A50I mutation in complex with mouse talin 1 helix 50 (H50, residues 2072-2103)

Method: X-RAY DIFFRACTION Dmax: 98.5 Å Quality: REASONABLE

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

Vinculin

Mus musculus

UniProt Q64727

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 A; UniProt 2–258 Mutation:A50I Talin-1 × 1 (P26039) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;292.15 K;100 mM Bis-tris pH 6.0, 15% PEG 3350 Resolution 1.49 Å R-free 0.235

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 VINC_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–260; UniProt 2–258

Talin-1

OrganismNot specified

UniProt P26039

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 2072–2103 Not recorded Vinculin × 1 (Q64727) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;292.15 K;100 mM Bis-tris pH 6.0, 15% PEG 3350 Resolution 1.49 Å R-free 0.235

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.

50 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLN1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–33; UniProt 2072–2103

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 9sr0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9sr0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9sr0
Deposition date deposition_date2025-09-23
最后修订 last_revision2026-05-20
Structure title titleMouse vinculin head domain 1 (VD1) (residues 2-258) with A50I mutation in complex with mouse talin 1 helix 50 (H50, residues 2072-2103)
Keywords keywordsvinculin, talin, vinculin binding site, focal adhesions, A50I, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.07
Radius of gyration Rg (electron density) rg_electron26.16
Forward intensity I(0) i015780800.00
Molecular weight molecular_weight30565.0 kDa
Excluded volume excluded_volume38579 ų
Envelope volume envelope_volume47764 ų
Hydration-shell volume shell_volume17849 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg28.85
Envelope Rg envelope_rg26.42
Shape Rg shape_rg26.17
Total Rg total_rg26.45
Total atoms total_atoms2139
Residues n_residues277
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 dmax98.5
Rg (real space) rg_real26.54
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.5780e+07
I(0) uncertainty (real space) i0_real_error2.4150e+05
Rg (reciprocal space) rg_reciprocal26.40
I(0) (reciprocal space) i0_reciprocal15780000.0000
Solution quality estimate total_estimate0.7370
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.0
Skewness Skewness skewness0.724
Kurtosis Kurtosis kurtosis0.052
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4277000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.455; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.228; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)