4f7g

Crystal structure of talin autoinhibition complex

Method: X-RAY DIFFRACTION Dmax: 84.9 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 206–405 Chain B; UniProt 1654–1847 Fragment:F2F3 subdomain, UNP residues 206-405 Fragment:RS subdomain, UNP residues 1654-1847 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;18.5% (w/v) PEG 1500, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;18.5% (w/v) PEG 1500, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.05 Å R-free 0.249

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 23–222; UniProt 206–405 Author chain B; PDBConstruct 23–216; UniProt 1654–1847

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 4f7g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4f7g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4f7g
Deposition date deposition_date2012-05-16
Structure title titleCrystal structure of talin autoinhibition complex
Keywords keywordsalpha-helix bundle, integrin activation, 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_guinier26.71
Radius of gyration Rg (electron density) rg_electron26.12
Forward intensity I(0) i026748500.00
Molecular weight molecular_weight39821.0 kDa
Excluded volume excluded_volume49951 ų
Envelope volume envelope_volume63429 ų
Hydration-shell volume shell_volume21779 ų
Envelope diameter envelope_diameter87.4
Shell Rg shell_rg31.46
Envelope Rg envelope_rg25.97
Shape Rg shape_rg26.13
Total Rg total_rg26.74
Total atoms total_atoms2797
Residues n_residues362
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 dmax84.9
Rg (real space) rg_real26.85
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.6750e+07
I(0) uncertainty (real space) i0_real_error4.1800e+05
Rg (reciprocal space) rg_reciprocal26.81
I(0) (reciprocal space) i0_reciprocal26750000.0000
Solution quality estimate total_estimate0.8802
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.371
Kurtosis Kurtosis kurtosis-0.626
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5118000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.785; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4f7ga1
Class classa — All alpha proteins
Fold Fold folda.11 — Acyl-CoA binding protein-like
Superfamily Superfamily superfamilya.11.2 — Second domain of FERM
Family Family familya.11.2.1 — Second domain of FERM
Domain ID domain_idd4f7ga2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.5 — Third domain of FERM

CATH v4.4 (3 domains)

Domain ID domain_id4f7gA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology80 — Acyl-CoA Binding Protein
Homologous superfamily homologous superfamily10
Domain ID domain_id4f7gA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id4f7gB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1420 — A middle domain of Talin 1
Homologous superfamily homologous superfamily10 — Talin, central domain

8. Citations (1)

9. Files and Curves (10)