8trl

T cell recognition of citrullinated alpha-enolase peptide presented by HLA-DR4

Method: X-RAY DIFFRACTION Dmax: 142.9 Å Quality: GOOD

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

HLA class II histocompatibility antigen, DR alpha chain

Homo sapiens

UniProt P01903

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 26–206 Fragment:UNP residues 26-206 HLA class II histocompatibility antigen, DRB1 beta chain × 1 (P01911) Alpha-enolase × 1 RA2.7 TCR alpha chain × 1 RA2.7 TCR beta chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ACT ACETATE ION × 2 FMT FORMIC ACID × 3 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;4-10% Tacsimate, 18-23% w/v PEG3350 Resolution 2.40 Å R-free 0.234
2 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 26–206 Fragment:UNP residues 26-206 HLA class II histocompatibility antigen, DRB1 beta chain × 1 (P01911) Alpha-enolase × 1 RA2.7 TCR alpha chain × 1 RA2.7 TCR beta chain × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ACT ACETATE ION × 1 FMT FORMIC ACID × 1 GOL GLYCEROL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;4-10% Tacsimate, 18-23% w/v PEG3350 Resolution 2.40 Å R-free 0.234

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.

139 other PDB entries and 218 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–181; UniProt 26–206 Author chain D; PDBConstruct 1–181; UniProt 26–206

HLA class II histocompatibility antigen, DRB1 beta chain

Homo sapiens

UniProt P01911

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 30–219 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Alpha-enolase × 1 RA2.7 TCR alpha chain × 1 RA2.7 TCR beta chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ACT ACETATE ION × 2 FMT FORMIC ACID × 3 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;4-10% Tacsimate, 18-23% w/v PEG3350 Resolution 2.40 Å R-free 0.234
2 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 30–219 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Alpha-enolase × 1 RA2.7 TCR alpha chain × 1 RA2.7 TCR beta chain × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ACT ACETATE ION × 1 FMT FORMIC ACID × 1 GOL GLYCEROL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;4-10% Tacsimate, 18-23% w/v PEG3350 Resolution 2.40 Å R-free 0.234

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–190; UniProt 30–219 Author chain E; PDBConstruct 1–190; UniProt 30–219

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 8trl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8trl
Deposition date deposition_date2023-08-09
Structure title titleT cell recognition of citrullinated alpha-enolase peptide presented by HLA-DR4
Keywords keywordsimmune receptor complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.01
Radius of gyration Rg (electron density) rg_electron42.91
Forward intensity I(0) i0478737000.00
Molecular weight molecular_weight177830.0 kDa
Excluded volume excluded_volume221180 ų
Envelope volume envelope_volume310000 ų
Hydration-shell volume shell_volume61140 ų
Envelope diameter envelope_diameter153.1
Shell Rg shell_rg46.51
Envelope Rg envelope_rg42.79
Shape Rg shape_rg42.92
Total Rg total_rg43.04
Total atoms total_atoms12574
Residues n_residues1607
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 dmax142.9
Rg (real space) rg_real42.94
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real4.7870e+08
I(0) uncertainty (real space) i0_real_error9.0060e+06
Rg (reciprocal space) rg_reciprocal43.01
I(0) (reciprocal space) i0_reciprocal478800000.0000
Solution quality estimate total_estimate0.8865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.9
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40790000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)