8zox

3D structure of Y-50 TCR-TMM-CD1b ternary complex

Method: ELECTRON MICROSCOPY Dmax: 131.4 Å Quality: GOOD

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

T-cell surface glycoprotein CD1b

Homo sapiens

UniProt P29016

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 18–295 Not recorded Beta-2-microglobulin × 1 (P61769) Y-50 TCR alpha × 1 Y-50 TCR beta × 1 6UL TETRACOSYL PALMITATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GLC alpha-D-glucopyranose × 1 A1L2B [(2R,3S,4S,5R,6S)-3,4,5,6-tetrakis(oxidanyl)oxan-2-yl]methyl (2R,3R)-3-oxidanyl-2-tetradecyl-octadecanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

27 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–280; UniProt 18–295

Beta-2-microglobulin

Homo sapiens

UniProt P61769

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded T-cell surface glycoprotein CD1b × 1 (P29016) Y-50 TCR alpha × 1 Y-50 TCR beta × 1 6UL TETRACOSYL PALMITATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GLC alpha-D-glucopyranose × 1 A1L2B [(2R,3S,4S,5R,6S)-3,4,5,6-tetrakis(oxidanyl)oxan-2-yl]methyl (2R,3R)-3-oxidanyl-2-tetradecyl-octadecanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

1313 other PDB entries and 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–100; UniProt 21–119

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 8zox

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8zox
Deposition date deposition_date2024-05-29
Structure title title3D structure of Y-50 TCR-TMM-CD1b ternary complex
Keywords keywordsIMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.80
Radius of gyration Rg (electron density) rg_electron38.13
Forward intensity I(0) i0258056000.00
Molecular weight molecular_weight87047.0 kDa
Excluded volume excluded_volume84342 ų
Envelope volume envelope_volume156000 ų
Hydration-shell volume shell_volume37386 ų
Envelope diameter envelope_diameter138.2
Shell Rg shell_rg39.70
Envelope Rg envelope_rg38.28
Shape Rg shape_rg38.12
Total Rg total_rg38.23
Total atoms total_atoms6590
Residues n_residues813
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 dmax131.4
Rg (real space) rg_real38.40
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real2.5810e+08
I(0) uncertainty (real space) i0_real_error5.0710e+06
Rg (reciprocal space) rg_reciprocal38.03
I(0) (reciprocal space) i0_reciprocal258000000.0000
Solution quality estimate total_estimate0.7891
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.637
Kurtosis Kurtosis kurtosis-0.203
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14960000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.670; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.720; Smooth: 0.525

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)