9jy3

delta epsilon/gamma epsilon Fab-TCR tetramer

Method: ELECTRON MICROSCOPY Dmax: 184.6 Å Quality: REASONABLE

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 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain A; UniProt 26–56 Chain B; UniProt 26–56 Chain a; UniProt 26–56 Chain b; UniProt 26–56 Not recorded T-cell surface glycoprotein CD3 delta chain × 2 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 4 (P07766) T-cell surface glycoprotein CD3 gamma chain × 2 (P09693) T cell receptor delta constant × 2 (B7Z8K6) T cell receptor gamma constant 1 × 2 (P0CF51) Fab light chain × 2 Fab heavy chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 1–31; UniProt 26–56 Author chain B; PDBConstruct 1–31; UniProt 26–56 Author chain a; PDBConstruct 1–31; UniProt 26–56 Author chain b; PDBConstruct 1–31; UniProt 26–56

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 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain D; UniProt 22–126 Chain d; UniProt 22–126 Not recorded T-cell surface glycoprotein CD3 zeta chain × 4 (P20963) T-cell surface glycoprotein CD3 epsilon chain × 4 (P07766) T-cell surface glycoprotein CD3 gamma chain × 2 (P09693) T cell receptor delta constant × 2 (B7Z8K6) T cell receptor gamma constant 1 × 2 (P0CF51) Fab light chain × 2 Fab heavy chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 1–105; UniProt 22–126 Author chain d; PDBConstruct 1–105; UniProt 22–126

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 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain E; UniProt 33–154 Chain F; UniProt 33–154 Chain e; UniProt 33–154 Chain f; UniProt 33–154 Not recorded T-cell surface glycoprotein CD3 zeta chain × 4 (P20963) T-cell surface glycoprotein CD3 delta chain × 2 (P04234) T-cell surface glycoprotein CD3 gamma chain × 2 (P09693) T cell receptor delta constant × 2 (B7Z8K6) T cell receptor gamma constant 1 × 2 (P0CF51) Fab light chain × 2 Fab heavy chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 1–122; UniProt 33–154 Author chain F; PDBConstruct 1–122; UniProt 33–154 Author chain e; PDBConstruct 1–122; UniProt 33–154 Author chain f; PDBConstruct 1–122; UniProt 33–154

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 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain G; UniProt 26–140 Chain g; UniProt 26–140 Not recorded T-cell surface glycoprotein CD3 zeta chain × 4 (P20963) T-cell surface glycoprotein CD3 delta chain × 2 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 4 (P07766) T cell receptor delta constant × 2 (B7Z8K6) T cell receptor gamma constant 1 × 2 (P0CF51) Fab light chain × 2 Fab heavy chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 1–115; UniProt 26–140 Author chain g; PDBConstruct 1–115; UniProt 26–140

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 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain M; UniProt 117–152 Chain m; UniProt 117–152 Not recorded T-cell surface glycoprotein CD3 zeta chain × 4 (P20963) T-cell surface glycoprotein CD3 delta chain × 2 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 4 (P07766) T-cell surface glycoprotein CD3 gamma chain × 2 (P09693) T cell receptor gamma constant 1 × 2 (P0CF51) Fab light chain × 2 Fab heavy chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 1–36; UniProt 117–152 Author chain m; PDBConstruct 1–36; UniProt 117–152

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 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain N; UniProt 127–164 Chain n; UniProt 127–164 Not recorded T-cell surface glycoprotein CD3 zeta chain × 4 (P20963) T-cell surface glycoprotein CD3 delta chain × 2 (P04234) T-cell surface glycoprotein CD3 epsilon chain × 4 (P07766) T-cell surface glycoprotein CD3 gamma chain × 2 (P09693) T cell receptor delta constant × 2 (B7Z8K6) Fab light chain × 2 Fab heavy chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 1–38; UniProt 127–164 Author chain n; PDBConstruct 1–38; UniProt 127–164

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 9jy3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jy3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jy3
Deposition date deposition_date2024-10-12
Structure title titledelta epsilon/gamma epsilon Fab-TCR tetramer
Keywords keywordsT cell receptor, gamma delta TCR, immune cell, Fab complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.73
Radius of gyration Rg (electron density) rg_electron58.54
Forward intensity I(0) i0671160000.00
Molecular weight molecular_weight222530.0 kDa
Excluded volume excluded_volume281080 ų
Envelope volume envelope_volume450560 ų
Hydration-shell volume shell_volume68328 ų
Envelope diameter envelope_diameter194.8
Shell Rg shell_rg54.45
Envelope Rg envelope_rg57.70
Shape Rg shape_rg58.52
Total Rg total_rg58.48
Total atoms total_atoms15638
Residues n_residues1998
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 dmax184.6
Rg (real space) rg_real57.20
Rg uncertainty (real space) rg_real_error2.43
I(0) (real space) i0_real6.7120e+08
I(0) uncertainty (real space) i0_real_error1.5670e+07
Rg (reciprocal space) rg_reciprocal56.31
I(0) (reciprocal space) i0_reciprocal670200000.0000
Solution quality estimate total_estimate0.5892
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39110000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 0.999; Sysdev: 0.041; Positv: 1.000; Valcen: 0.871; Smooth: 0.045

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)