8ivz

Crystal structure of talin R7 in complex with KANK1 KN motif

Method: X-RAY DIFFRACTION Dmax: 153.9 Å Quality: REASONABLE

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1357–1653 Not recorded KN motif and ankyrin repeat domains 1 × 2 (A0A8J9BYE6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;25% w/v pentaerythritol ethoxylate, 50 mM Magnesium chloride, 10 mM Tris pH8.5 Resolution 2.80 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1357–1653 Not recorded KN motif and ankyrin repeat domains 1 × 2 (A0A8J9BYE6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;25% w/v pentaerythritol ethoxylate, 50 mM Magnesium chloride, 10 mM Tris pH8.5 Resolution 2.80 Å R-free 0.264

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 5–171; UniProt 1357–1653 Author chain B; PDBConstruct 5–171; UniProt 1357–1653

KN motif and ankyrin repeat domains 1

Homo sapiens

UniProt A0A8J9BYE6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 30–55 Not recorded Talin-1 × 2 (P26039) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;25% w/v pentaerythritol ethoxylate, 50 mM Magnesium chloride, 10 mM Tris pH8.5 Resolution 2.80 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 30–55 Not recorded Talin-1 × 2 (P26039) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;25% w/v pentaerythritol ethoxylate, 50 mM Magnesium chloride, 10 mM Tris pH8.5 Resolution 2.80 Å R-free 0.264

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 A0A8J9BYE6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–26; UniProt 30–55 Author chain D; PDBConstruct 1–26; UniProt 30–55

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 8ivz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ivz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ivz
Deposition date deposition_date2023-03-29
Structure title titleCrystal structure of talin R7 in complex with KANK1 KN motif
Keywords keywordsFocal adhesion, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.38
Radius of gyration Rg (electron density) rg_electron42.28
Forward intensity I(0) i028175700.00
Molecular weight molecular_weight40620.0 kDa
Excluded volume excluded_volume50495 ų
Envelope volume envelope_volume97520 ų
Hydration-shell volume shell_volume23455 ų
Envelope diameter envelope_diameter158.7
Shell Rg shell_rg38.98
Envelope Rg envelope_rg40.71
Shape Rg shape_rg42.27
Total Rg total_rg42.03
Total atoms total_atoms2847
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 dmax153.9
Rg (real space) rg_real43.20
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.8340e+07
I(0) uncertainty (real space) i0_real_error4.8240e+05
Rg (reciprocal space) rg_reciprocal41.39
I(0) (reciprocal space) i0_reciprocal28150000.0000
Solution quality estimate total_estimate0.5381
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.6
Skewness Skewness skewness0.638
Kurtosis Kurtosis kurtosis-0.083
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha1.0280
Highest regularization parameter α highest_alpha1246000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.438; Stabil: 0.904; Sysdev: 0.000; Positv: 1.000; Valcen: 0.632; Smooth: 0.347

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)