1r5v

X-ray diffraction
2.5Å resolution

Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero hexamer
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
H-2 class II histocompatibility antigen, E-K alpha chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 180 amino acids
Theoretical weight: 20.96 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04224 (Residues: 28-207; Coverage: 78%)
Sequence domains:
Structure domains:
artificial peptide Chains: E, F
Molecule details ›
Chains: E, F
Length: 13 amino acids
Theoretical weight: 1.41 KDa
H-2 class II histocompatibility antigen, I-A beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 185 amino acids
Theoretical weight: 21.74 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P18468 (Residues: 32-215; Coverage: 79%)
Gene name: H2-Eb1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 79.42Å b: 104.65Å c: 120.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.241
Expression system: Escherichia coli