9qn7

Structure of talin in complex with a peptide fragment

Method: X-RAY DIFFRACTION Dmax: 120.5 Å Quality: GOOD

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

Talin-1

Mus musculus

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 A; UniProt 1974–2293 Not recorded Tensin-3 × 1 (Q68CZ2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.4;294.15 K;0.9M sodium potassium tartrate tetrathydrate, 20% w/v glycerol, 0.05M HEPES pH 7.4 Resolution 2.76 Å R-free 0.296
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1974–2293 Not recorded Tensin-3 × 1 (Q68CZ2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.4;294.15 K;0.9M sodium potassium tartrate tetrathydrate, 20% w/v glycerol, 0.05M HEPES pH 7.4 Resolution 2.76 Å R-free 0.296

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 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLN1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–330; UniProt 1974–2293 Author chain B; PDBConstruct 11–330; UniProt 1974–2293

Tensin-3

OrganismNot specified

UniProt Q68CZ2

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 C; UniProt 692–718 Not recorded Talin-1 × 1 (P26039) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.4;294.15 K;0.9M sodium potassium tartrate tetrathydrate, 20% w/v glycerol, 0.05M HEPES pH 7.4 Resolution 2.76 Å R-free 0.296
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 692–718 Not recorded Talin-1 × 1 (P26039) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.4;294.15 K;0.9M sodium potassium tartrate tetrathydrate, 20% w/v glycerol, 0.05M HEPES pH 7.4 Resolution 2.76 Å R-free 0.296

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 TENS3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–27; UniProt 692–718 Author chain D; PDBConstruct 1–27; UniProt 692–718

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 9qn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qn7
Deposition date deposition_date2025-03-24
Structure title titleStructure of talin in complex with a peptide fragment
Keywords keywordstalin, tensin3, phase seperation, adhesion, 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_guinier36.27
Radius of gyration Rg (electron density) rg_electron35.91
Forward intensity I(0) i083589700.00
Molecular weight molecular_weight72459.0 kDa
Excluded volume excluded_volume90652 ų
Envelope volume envelope_volume128390 ų
Hydration-shell volume shell_volume31044 ų
Envelope diameter envelope_diameter127.0
Shell Rg shell_rg40.88
Envelope Rg envelope_rg34.77
Shape Rg shape_rg35.92
Total Rg total_rg36.25
Total atoms total_atoms5076
Residues n_residues684
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 dmax120.5
Rg (real space) rg_real36.28
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real8.3590e+07
I(0) uncertainty (real space) i0_real_error1.2970e+06
Rg (reciprocal space) rg_reciprocal36.28
I(0) (reciprocal space) i0_reciprocal83590000.0000
Solution quality estimate total_estimate0.8530
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.0
Skewness Skewness skewness0.193
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4422000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.785; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.801

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)