› 3o3a

X-ray diffraction
1.8Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-137753 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HLA class I histocompatibility antigen, A alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 275 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04439 (Residues: 25-299; Coverage: 81%)
Gene names: HLA-A, HLAA
Sequence domains:
Structure domains:
Beta-2-microglobulin Chains: B, E
Molecule details ›
Chains: B, E
Length: 100 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Peptidomimetic ELA-1 Chains: C, F
Molecule details ›
Chains: C, F
Length: 8 amino acids
Theoretical weight: 977 Da

Ligands and Environments

1 bound ligand:
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 58.208Å b: 84.222Å c: 83.946Å
α: 90° β: 89.96° γ: 90°
R-values:
R R work R free
0.173 0.171 0.212
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism.
Baker et al. (2012)
2 more

2 mentions without citation

Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope.
Song et al. (2017)
1 more