9jy2

Fab-CD3-delta epsilon-TCR complex

Method: ELECTRON MICROSCOPY Dmax: 126.5 Å Quality: GOOD

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain a; UniProt 26–56 Chain b; UniProt 26–56 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 constant × 1 (B7Z8K6) T cell receptor gamma constant 1 × 1 (P0CF51) Fab light chain × 1 Fab heavy chain × 1 CLR CHOLESTEROL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain d; UniProt 22–126 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 constant × 1 (B7Z8K6) T cell receptor gamma constant 1 × 1 (P0CF51) Fab light chain × 1 Fab heavy chain × 1 CLR CHOLESTEROL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain e; UniProt 33–154 Chain f; UniProt 33–154 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 constant × 1 (B7Z8K6) T cell receptor gamma constant 1 × 1 (P0CF51) Fab light chain × 1 Fab heavy chain × 1 CLR CHOLESTEROL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain g; UniProt 26–140 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 constant × 1 (B7Z8K6) T cell receptor gamma constant 1 × 1 (P0CF51) Fab light chain × 1 Fab heavy chain × 1 CLR CHOLESTEROL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain m; UniProt 117–152 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 constant 1 × 1 (P0CF51) Fab light chain × 1 Fab heavy chain × 1 CLR CHOLESTEROL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain n; UniProt 127–164 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 constant × 1 (B7Z8K6) Fab light chain × 1 Fab heavy chain × 1 CLR CHOLESTEROL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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

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 9jy2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jy2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jy2
Deposition date deposition_date2024-10-12
Structure title titleFab-CD3-delta epsilon-TCR complex
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_guinier37.63
Radius of gyration Rg (electron density) rg_electron38.28
Forward intensity I(0) i0122130000.00
Molecular weight molecular_weight92733.0 kDa
Excluded volume excluded_volume117520 ų
Envelope volume envelope_volume156590 ų
Hydration-shell volume shell_volume36351 ų
Envelope diameter envelope_diameter135.1
Shell Rg shell_rg40.92
Envelope Rg envelope_rg37.97
Shape Rg shape_rg38.32
Total Rg total_rg38.34
Total atoms total_atoms6515
Residues n_residues818
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 dmax126.5
Rg (real space) rg_real37.86
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.2210e+08
I(0) uncertainty (real space) i0_real_error2.4430e+06
Rg (reciprocal space) rg_reciprocal37.73
I(0) (reciprocal space) i0_reciprocal122100000.0000
Solution quality estimate total_estimate0.8657
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11620000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.877; Smooth: 0.733

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)