8vte

Co-structure of the Fab of the anti-TIGIT Vibostolimab antibody with its antigen

Method: X-RAY DIFFRACTION Dmax: 108.2 Å Quality: GOOD

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

T-cell immunoreceptor with Ig and ITIM domains

Homo sapiens

UniProt Q495A1

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 22–137 Not recorded Tiragolumab antibody light chain variable domains × 1 Tiragolumab antibody heavy chain variable domains × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;300 K;0.02M D-Glucose; 0.02M D-Mannose; 0.02M D-Galactose; 0.02M L-Fucose; 0.02M D-Xylose; 0.02M N-Acetyl-D-Glucosamine; 0.1M Imidazole, 0.1M MES; 20%v/v Glycerol; 10% PEG4K Resolution 2.29 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 22–137 Not recorded Tiragolumab antibody light chain variable domains × 1 Tiragolumab antibody heavy chain variable domains × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;300 K;0.02M D-Glucose; 0.02M D-Mannose; 0.02M D-Galactose; 0.02M L-Fucose; 0.02M D-Xylose; 0.02M N-Acetyl-D-Glucosamine; 0.1M Imidazole, 0.1M MES; 20%v/v Glycerol; 10% PEG4K Resolution 2.29 Å R-free 0.268

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.

11 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIGIT_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–116; UniProt 22–137 Author chain F; PDBConstruct 1–116; UniProt 22–137

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 8vte

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vte
Deposition date deposition_date2024-01-26
Structure title titleCo-structure of the Fab of the anti-TIGIT Vibostolimab antibody with its antigen
Keywords keywordsantibody TIGIT immunotherapy, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.40
Radius of gyration Rg (electron density) rg_electron32.55
Forward intensity I(0) i0225559000.00
Molecular weight molecular_weight119350.0 kDa
Excluded volume excluded_volume148980 ų
Envelope volume envelope_volume197210 ų
Hydration-shell volume shell_volume50033 ų
Envelope diameter envelope_diameter114.4
Shell Rg shell_rg40.01
Envelope Rg envelope_rg32.17
Shape Rg shape_rg32.51
Total Rg total_rg33.26
Total atoms total_atoms16575
Residues n_residues1098
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 dmax108.2
Rg (real space) rg_real33.24
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.2560e+08
I(0) uncertainty (real space) i0_real_error3.2050e+06
Rg (reciprocal space) rg_reciprocal33.34
I(0) (reciprocal space) i0_reciprocal225600000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.8
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26750000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)