8jen

Crystal structure of TIGIT in complexed with Ociperlimab, crystal form II

Method: X-RAY DIFFRACTION Dmax: 154.1 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 I; UniProt 22–128 Not recorded antibody heavy chain × 1 antibody light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium citrate tribasic dihydrate pH 5.2, 17% PEG 20000 Resolution 2.71 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 22–128 Not recorded antibody heavy chain × 1 antibody light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium citrate tribasic dihydrate pH 5.2, 17% PEG 20000 Resolution 2.71 Å R-free 0.289
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 22–128 Not recorded antibody heavy chain × 1 antibody light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium citrate tribasic dihydrate pH 5.2, 17% PEG 20000 Resolution 2.71 Å R-free 0.289
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 22–128 Not recorded antibody heavy chain × 1 antibody light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium citrate tribasic dihydrate pH 5.2, 17% PEG 20000 Resolution 2.71 Å R-free 0.289

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 21 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 I; PDBConstruct 1–107; UniProt 22–128 Author chain J; PDBConstruct 1–107; UniProt 22–128 Author chain M; PDBConstruct 1–107; UniProt 22–128 Author chain P; PDBConstruct 1–107; UniProt 22–128

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 8jen

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8jen
Deposition date deposition_date2023-05-16
Structure title titleCrystal structure of TIGIT in complexed with Ociperlimab, crystal form II
Keywords keywordsimmunotherapy, antibody, checkpoint inhibitor, 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_guinier47.41
Radius of gyration Rg (electron density) rg_electron46.99
Forward intensity I(0) i0804313000.00
Molecular weight molecular_weight232090.0 kDa
Excluded volume excluded_volume289220 ų
Envelope volume envelope_volume428110 ų
Hydration-shell volume shell_volume76613 ų
Envelope diameter envelope_diameter160.5
Shell Rg shell_rg50.99
Envelope Rg envelope_rg45.52
Shape Rg shape_rg46.96
Total Rg total_rg47.27
Total atoms total_atoms16341
Residues n_residues2146
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 dmax154.1
Rg (real space) rg_real47.24
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real8.0430e+08
I(0) uncertainty (real space) i0_real_error1.6340e+07
Rg (reciprocal space) rg_reciprocal47.41
I(0) (reciprocal space) i0_reciprocal804500000.0000
Solution quality estimate total_estimate0.8830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.7
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44050000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)