8jbv

Extracellular domain of gamma delta TCR

Method: ELECTRON MICROSCOPY Dmax: 124.3 Å Quality: GOOD

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

T cell receptor delta variable 1,T cell receptor delta constant

Homo sapiens

UniProt A0A1B0GX56

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 Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 21–114 Chain m; UniProt 21–114 Not recorded T cell receptor gamma variable 5,T cell receptor gamma constant 1 × 2 (A0A0B4J1U4,P0CF51) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 Resolution 3.02 Å

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRDV1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain M; PDBConstruct 38–131; UniProt 21–114 Author chain m; PDBConstruct 38–131; UniProt 21–114

T cell receptor delta variable 1,T cell receptor delta constant

Homo sapiens

UniProt B7Z8K6

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 Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 1–153 Chain m; UniProt 1–153 Not recorded T cell receptor gamma variable 5,T cell receptor gamma constant 1 × 2 (A0A0B4J1U4,P0CF51) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 Resolution 3.02 Å

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRDC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain M; PDBConstruct 155–307; UniProt 1–153 Author chain m; PDBConstruct 155–307; UniProt 1–153

T cell receptor gamma variable 5,T cell receptor gamma constant 1

Homo sapiens

UniProt A0A0B4J1U4

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 Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N; UniProt 19–118 Chain n; UniProt 19–118 Not recorded T cell receptor delta variable 1,T cell receptor delta constant × 2 (A0A1B0GX56,B7Z8K6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 Resolution 3.02 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRGV5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 38–137; UniProt 19–118 Author chain n; PDBConstruct 38–137; UniProt 19–118

T cell receptor gamma variable 5,T cell receptor gamma constant 1

Homo sapiens

UniProt P0CF51

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 Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N; UniProt 1–173 Chain n; UniProt 1–173 Not recorded T cell receptor delta variable 1,T cell receptor delta constant × 2 (A0A1B0GX56,B7Z8K6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 Resolution 3.02 Å

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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRGC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 159–331; UniProt 1–173 Author chain n; PDBConstruct 159–331; UniProt 1–173

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 8jbv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8jbv
Deposition date deposition_date2023-05-09
Structure title titleExtracellular domain of gamma delta TCR
Keywords keywordsReceptor, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.98
Radius of gyration Rg (electron density) rg_electron37.80
Forward intensity I(0) i0128386000.00
Molecular weight molecular_weight93948.0 kDa
Excluded volume excluded_volume118670 ų
Envelope volume envelope_volume167690 ų
Hydration-shell volume shell_volume38392 ų
Envelope diameter envelope_diameter125.9
Shell Rg shell_rg42.15
Envelope Rg envelope_rg37.19
Shape Rg shape_rg37.77
Total Rg total_rg38.21
Total atoms total_atoms6624
Residues n_residues824
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 dmax124.3
Rg (real space) rg_real38.13
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real1.2840e+08
I(0) uncertainty (real space) i0_real_error2.2400e+06
Rg (reciprocal space) rg_reciprocal38.04
I(0) (reciprocal space) i0_reciprocal128400000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.656
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12170000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)