9jxz

V gamma9 V delta2 TCR and CD3 complex

Method: ELECTRON MICROSCOPY Dmax: 102.8 Å Quality: EXCELLENT

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

T-cell surface glycoprotein CD3 zeta chain

Homo sapiens

UniProt P20963

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain a; UniProt 1–164 Chain b; UniProt 1–164 Not recorded T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor delta variable 2,T cell receptor delta constant × 1 (A0JD36,B7Z8K6) T cell receptor gamma variable 9,T cell receptor gamma constant 1 × 1 (Q99603,P0CF51) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

36 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD3Z_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–164; UniProt 1–164 Author chain b; PDBConstruct 1–164; UniProt 1–164

T-cell surface glycoprotein CD3 delta chain

Homo sapiens

UniProt P04234

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain d; UniProt 1–171 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor delta variable 2,T cell receptor delta constant × 1 (A0JD36,B7Z8K6) T cell receptor gamma variable 9,T cell receptor gamma constant 1 × 1 (Q99603,P0CF51) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD3D_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain d; PDBConstruct 1–171; UniProt 1–171

T-cell surface glycoprotein CD3 epsilon chain

Homo sapiens

UniProt P07766

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain e; UniProt 1–207 Chain f; UniProt 1–207 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor delta variable 2,T cell receptor delta constant × 1 (A0JD36,B7Z8K6) T cell receptor gamma variable 9,T cell receptor gamma constant 1 × 1 (Q99603,P0CF51) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

42 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD3E_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain e; PDBConstruct 1–207; UniProt 1–207 Author chain f; PDBConstruct 1–207; UniProt 1–207

T-cell surface glycoprotein CD3 gamma chain

Homo sapiens

UniProt P09693

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain g; UniProt 1–182 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T cell receptor delta variable 2,T cell receptor delta constant × 1 (A0JD36,B7Z8K6) T cell receptor gamma variable 9,T cell receptor gamma constant 1 × 1 (Q99603,P0CF51) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD3G_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain g; PDBConstruct 1–182; UniProt 1–182

T cell receptor delta variable 2,T cell receptor delta constant

Homo sapiens

UniProt A0JD36

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain m; UniProt 1–115 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor gamma variable 9,T cell receptor gamma constant 1 × 1 (Q99603,P0CF51) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 TRDV2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain m; PDBConstruct 1–115; UniProt 1–115

T cell receptor delta variable 2,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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain m; UniProt 1–153 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor gamma variable 9,T cell receptor gamma constant 1 × 1 (Q99603,P0CF51) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 5
Chains and sequence ranges Author chain m; PDBConstruct 140–292; UniProt 1–153

T cell receptor gamma variable 9,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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain n; UniProt 1–173 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor delta variable 2,T cell receptor delta constant × 1 (A0JD36,B7Z8K6) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 6
Chains and sequence ranges Author chain n; PDBConstruct 143–315; UniProt 1–173

T cell receptor gamma variable 9,T cell receptor gamma constant 1

Homo sapiens

UniProt Q99603

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain n; UniProt 1–121 Not recorded T-cell surface glycoprotein CD3 zeta chain × 2 (P20963) T-cell surface glycoprotein CD3 delta chain × 1 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 2 (P07766) T-cell surface glycoprotein CD3 gamma chain × 1 (P09693) T cell receptor delta variable 2,T cell receptor delta constant × 1 (A0JD36,B7Z8K6) CLR CHOLESTEROL × 2 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRGV9_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain n; PDBConstruct 1–121; UniProt 1–121

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 9jxz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jxz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jxz
Deposition date deposition_date2024-10-12
Structure title titleV gamma9 V delta2 TCR and CD3 complex
Keywords keywordsT cell receptor, gamma delta TCR, immune cell, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.87
Radius of gyration Rg (electron density) rg_electron31.63
Forward intensity I(0) i067999500.00
Molecular weight molecular_weight69089.0 kDa
Excluded volume excluded_volume88263 ų
Envelope volume envelope_volume116090 ų
Hydration-shell volume shell_volume31984 ų
Envelope diameter envelope_diameter106.5
Shell Rg shell_rg36.83
Envelope Rg envelope_rg31.40
Shape Rg shape_rg31.70
Total Rg total_rg31.93
Total atoms total_atoms4846
Residues n_residues597
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 dmax102.8
Rg (real space) rg_real31.90
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real6.8000e+07
I(0) uncertainty (real space) i0_real_error9.8460e+05
Rg (reciprocal space) rg_reciprocal31.89
I(0) (reciprocal space) i0_reciprocal68000000.0000
Solution quality estimate total_estimate0.9026
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.9
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.628
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha11160000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)