9c1t

Crystal structure of integrin beta-3 tail bound to the FERM-folded talin head domain with a D397R mutation

Method: X-RAY DIFFRACTION Dmax: 106.0 Å Quality: GOOD

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

Integrin beta-3, 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–430 Mutation:D397R SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M sodium chloride, 0.1 M MES pH6.5, 10 % w/v PEG 4000 Resolution 2.30 Å R-free 0.267

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 1
Chains and sequence ranges Author chain A; PDBConstruct 12–411; UniProt 1–430

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 9c1t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c1t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c1t
Deposition date deposition_date2024-05-29
Structure title titleCrystal structure of integrin beta-3 tail bound to the FERM-folded talin head domain with a D397R mutation
Keywords keywordsTalin, integrin, FERM, beta3, 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_guinier28.08
Radius of gyration Rg (electron density) rg_electron27.59
Forward intensity I(0) i031107800.00
Molecular weight molecular_weight43065.0 kDa
Excluded volume excluded_volume54044 ų
Envelope volume envelope_volume72842 ų
Hydration-shell volume shell_volume24064 ų
Envelope diameter envelope_diameter109.7
Shell Rg shell_rg31.77
Envelope Rg envelope_rg28.74
Shape Rg shape_rg27.54
Total Rg total_rg28.24
Total atoms total_atoms3024
Residues n_residues378
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 dmax106.0
Rg (real space) rg_real28.47
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real3.1110e+07
I(0) uncertainty (real space) i0_real_error5.4750e+05
Rg (reciprocal space) rg_reciprocal28.35
I(0) (reciprocal space) i0_reciprocal31110000.0000
Solution quality estimate total_estimate0.7847
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary104.1
Skewness Skewness skewness0.653
Kurtosis Kurtosis kurtosis0.179
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9206000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.597; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.477; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)