7rdv

TFH TCR bound to MHC Class II IAd presenting aggrecan epitope

Method: X-RAY DIFFRACTION Dmax: 128.3 Å Quality: GOOD

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

H-2 class II histocompatibility antigen, A-D alpha chain

Mus musculus

UniProt P04228

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 28–205 Not recorded H-2 class II histocompatibility antigen, A-D beta chain × 1 (P01921) TFH TCR alpha chain × 1 TFH TCR beta chain × 1 Aggrecan core peptide × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293.15 K;0.1M Sodium Cacodylate pH6.0 15% w/v PEG4000 Resolution 2.90 Å R-free 0.265

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA2D_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–178; UniProt 28–205

H-2 class II histocompatibility antigen, A-D beta chain

Mus musculus

UniProt P01921

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 31–216 Not recorded H-2 class II histocompatibility antigen, A-D alpha chain × 1 (P04228) TFH TCR alpha chain × 1 TFH TCR beta chain × 1 Aggrecan core peptide × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293.15 K;0.1M Sodium Cacodylate pH6.0 15% w/v PEG4000 Resolution 2.90 Å R-free 0.265

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HB2D_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–186; UniProt 31–216

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 7rdv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rdv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7rdv
Deposition date deposition_date2021-07-11
Structure title titleTFH TCR bound to MHC Class II IAd presenting aggrecan epitope
Keywords keywordsImmune receptor, MHC class II, 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_guinier35.16
Radius of gyration Rg (electron density) rg_electron35.43
Forward intensity I(0) i0120761000.00
Molecular weight molecular_weight85513.0 kDa
Excluded volume excluded_volume105690 ų
Envelope volume envelope_volume141840 ų
Hydration-shell volume shell_volume36060 ų
Envelope diameter envelope_diameter137.6
Shell Rg shell_rg38.12
Envelope Rg envelope_rg36.35
Shape Rg shape_rg35.43
Total Rg total_rg35.63
Total atoms total_atoms6045
Residues n_residues783
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 dmax128.3
Rg (real space) rg_real35.64
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real1.2080e+08
I(0) uncertainty (real space) i0_real_error2.2690e+06
Rg (reciprocal space) rg_reciprocal35.34
I(0) (reciprocal space) i0_reciprocal120700000.0000
Solution quality estimate total_estimate0.7828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.681
Kurtosis Kurtosis kurtosis-0.022
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19000000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.580; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.583; Smooth: 0.848

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7rdvC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)