3q0h

Structure of T-cell immunoreceptor with immunoglobulin and ITIM domains (TIGIT)

Method: X-RAY DIFFRACTION Dmax: 72.0 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 22–137 Fragment:Ig-like V-type domain residues 22-137 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;1.3M Ammonium Sulfate, 0.1M MES pH 6.0, Vapor diffusion, Sitting drop, temperature 298K Resolution 1.70 Å R-free 0.237
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–137 Fragment:Ig-like V-type domain residues 22-137 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;1.3M Ammonium Sulfate, 0.1M MES pH 6.0, Vapor diffusion, Sitting drop, temperature 298K Resolution 1.70 Å R-free 0.237

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 1
Chains and sequence ranges Author chain A; PDBConstruct 2–117; UniProt 22–137 Author chain B; PDBConstruct 2–117; 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 3q0h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3q0h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3q0h
Deposition date deposition_date2010-12-15
Structure title titleStructure of T-cell immunoreceptor with immunoglobulin and ITIM domains (TIGIT)
Keywords keywords;Immune receptor, adhesion, Structural Genomics, New York Structural Genomics Research Consortium, NYSGRC, PSI-BIOLOGY, 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_guinier20.17
Radius of gyration Rg (electron density) rg_electron19.38
Forward intensity I(0) i010274700.00
Molecular weight molecular_weight23442.0 kDa
Excluded volume excluded_volume29161 ų
Envelope volume envelope_volume35215 ų
Hydration-shell volume shell_volume16086 ų
Envelope diameter envelope_diameter72.6
Shell Rg shell_rg24.49
Envelope Rg envelope_rg19.73
Shape Rg shape_rg19.31
Total Rg total_rg20.38
Total atoms total_atoms1648
Residues n_residues216
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 dmax72.0
Rg (real space) rg_real20.18
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.0270e+07
I(0) uncertainty (real space) i0_real_error1.3370e+05
Rg (reciprocal space) rg_reciprocal20.18
I(0) (reciprocal space) i0_reciprocal10270000.0000
Solution quality estimate total_estimate0.8589
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.291
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2297000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3q0ha1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd3q0ha2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3q0hb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3q0hA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3q0hB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)