7ceb

Crystal structure of alpha6beta1 integrin headpiece

Method: X-RAY DIFFRACTION Dmax: 138.7 Å Quality: GOOD

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

Integrin alpha-6

Homo sapiens

UniProt P23229

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 24–641 Not recorded Integrin beta-1 × 1 (P05556) TS2/16 VH(S112C)-SARAH × 1 TS2/16 VL-SARAH(S37C) × 1 CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;23% PEG1000, 0.2 M NaCl, 0.1 M Na/K phosphate, pH 6.5 Resolution 2.89 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITA6_HUMAN
Isoform P23229-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–618; UniProt 24–641

Integrin beta-1

Homo sapiens

UniProt P05556

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 B; UniProt 21–465 Not recorded Integrin alpha-6 × 1 (P23229) TS2/16 VH(S112C)-SARAH × 1 TS2/16 VL-SARAH(S37C) × 1 CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;23% PEG1000, 0.2 M NaCl, 0.1 M Na/K phosphate, pH 6.5 Resolution 2.89 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.

21 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 21–465

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 7ceb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ceb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ceb
Deposition date deposition_date2020-06-22
Structure title titleCrystal structure of alpha6beta1 integrin headpiece
Keywords keywordsIntegrin, Fv-clasp, Laminin, CELL ADHESION, CELL ADHESION-IMMUNE SYSTEM complex; CELL ADHESION/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.47
Radius of gyration Rg (electron density) rg_electron39.36
Forward intensity I(0) i0291723000.00
Molecular weight molecular_weight137110.0 kDa
Excluded volume excluded_volume170940 ų
Envelope volume envelope_volume230880 ų
Hydration-shell volume shell_volume50093 ų
Envelope diameter envelope_diameter149.1
Shell Rg shell_rg43.43
Envelope Rg envelope_rg39.87
Shape Rg shape_rg39.30
Total Rg total_rg39.81
Total atoms total_atoms9629
Residues n_residues1212
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 dmax138.7
Rg (real space) rg_real39.71
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real2.9170e+08
I(0) uncertainty (real space) i0_real_error5.8890e+06
Rg (reciprocal space) rg_reciprocal39.57
I(0) (reciprocal space) i0_reciprocal291700000.0000
Solution quality estimate total_estimate0.8548
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.6
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.170
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40550000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.892; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)