9ci8

T cell receptor complex

Method: ELECTRON MICROSCOPY Dmax: 186.2 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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain a; UniProt 27–57 Chain b; UniProt 27–57 Not recorded UCHT1 Fab × 2 UCHT1 Fab chain 2 × 2 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 (A0A075B6X2) T cell receptor gamma constant 1 × 1 (P0CF51) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Hepes buffer saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 3
Chains and sequence ranges Author chain a; PDBConstruct 1–31; UniProt 27–57 Author chain b; PDBConstruct 1–31; UniProt 27–57

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain d; UniProt 22–126 Not recorded UCHT1 Fab × 2 UCHT1 Fab chain 2 × 2 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 (A0A075B6X2) T cell receptor gamma constant 1 × 1 (P0CF51) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Hepes buffer saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 4
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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain e; UniProt 33–156 Chain f; UniProt 33–156 Not recorded UCHT1 Fab × 2 UCHT1 Fab chain 2 × 2 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 (A0A075B6X2) T cell receptor gamma constant 1 × 1 (P0CF51) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Hepes buffer saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 5
Chains and sequence ranges Author chain e; PDBConstruct 1–124; UniProt 33–156 Author chain f; PDBConstruct 1–124; UniProt 33–156

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain g; UniProt 24–138 Not recorded UCHT1 Fab × 2 UCHT1 Fab chain 2 × 2 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 (A0A075B6X2) T cell receptor gamma constant 1 × 1 (P0CF51) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Hepes buffer saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 6
Chains and sequence ranges Author chain g; PDBConstruct 1–115; UniProt 24–138

T cell receptor delta constant

Homo sapiens

UniProt A0A075B6X2

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain m; UniProt 119–154 Not recorded UCHT1 Fab × 2 UCHT1 Fab chain 2 × 2 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Hepes buffer saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A075B6X2_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain m; PDBConstruct 1–36; UniProt 119–154

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain n; UniProt 128–165 Not recorded UCHT1 Fab × 2 UCHT1 Fab chain 2 × 2 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 (A0A075B6X2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Hepes buffer saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 8
Chains and sequence ranges Author chain n; PDBConstruct 1–38; UniProt 128–165

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 9ci8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ci8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ci8
Deposition date deposition_date2024-07-02
Structure title titleT cell receptor complex
Keywords keywordsT cell receptor T cell immunity, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.56
Radius of gyration Rg (electron density) rg_electron54.38
Forward intensity I(0) i0310456000.00
Molecular weight molecular_weight148790.0 kDa
Excluded volume excluded_volume187140 ų
Envelope volume envelope_volume285990 ų
Hydration-shell volume shell_volume47252 ų
Envelope diameter envelope_diameter175.2
Shell Rg shell_rg50.80
Envelope Rg envelope_rg53.83
Shape Rg shape_rg54.39
Total Rg total_rg54.22
Total atoms total_atoms10466
Residues n_residues1382
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 dmax186.2
Rg (real space) rg_real53.81
Rg uncertainty (real space) rg_real_error2.56
I(0) (real space) i0_real3.1050e+08
I(0) uncertainty (real space) i0_real_error6.7130e+06
Rg (reciprocal space) rg_reciprocal53.33
I(0) (reciprocal space) i0_reciprocal310200000.0000
Solution quality estimate total_estimate0.8177
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.832
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10710000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.705; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.725; Smooth: 0.786

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)