8fse

Crystal structure of integrin beta-2 tail bound to the FERM-folded talin head domain

Method: X-RAY DIFFRACTION Dmax: 130.8 Å Quality: GOOD

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

Integrin beta-2,Talin-1

Mus musculus

UniProt P11835

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 750–759 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;300 K;PEG4000 16%, NaCl 0.1M, DTT 2mM Resolution 1.90 Å R-free 0.220
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 750–759 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;300 K;PEG4000 16%, NaCl 0.1M, DTT 2mM Resolution 1.90 Å R-free 0.220

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–11; UniProt 750–759 Author chain B; PDBConstruct 2–11; UniProt 750–759

Integrin beta-2,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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–430 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;300 K;PEG4000 16%, NaCl 0.1M, DTT 2mM Resolution 1.90 Å R-free 0.220
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–430 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;300 K;PEG4000 16%, NaCl 0.1M, DTT 2mM Resolution 1.90 Å R-free 0.220

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 12–411; UniProt 1–430 Author chain B; 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 8fse

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fse
Deposition date deposition_date2023-01-09
Structure title titleCrystal structure of integrin beta-2 tail bound to the FERM-folded talin head domain
Keywords keywordsintegrin, beta-2, talin, FERM, complex, 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_guinier33.87
Radius of gyration Rg (electron density) rg_electron33.09
Forward intensity I(0) i0115926000.00
Molecular weight molecular_weight86390.0 kDa
Excluded volume excluded_volume108690 ų
Envelope volume envelope_volume156910 ų
Hydration-shell volume shell_volume39589 ų
Envelope diameter envelope_diameter136.1
Shell Rg shell_rg39.66
Envelope Rg envelope_rg33.12
Shape Rg shape_rg33.05
Total Rg total_rg33.78
Total atoms total_atoms6069
Residues n_residues756
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 dmax130.8
Rg (real space) rg_real33.85
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real1.1590e+08
I(0) uncertainty (real space) i0_real_error2.0700e+06
Rg (reciprocal space) rg_reciprocal33.86
I(0) (reciprocal space) i0_reciprocal115900000.0000
Solution quality estimate total_estimate0.8003
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.5
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis0.067
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16000000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.504; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)