› 3skn

X-ray diffraction
2.9Å resolution

Crystal structure of the RL42 TCR unliganded

Released:
DOI: 10.2210/pdb3skn/pdb
PDB entry 3skn coloured by chain, front view.
PDB entry 3skn coloured by chain, side view.
PDB entry 3skn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A structural basis for varied αβ TCR usage against an immunodominant EBV antigen restricted to a HLA-B8 molecule.
Gras S, Wilmann PG, Chen Z, Halim H, Liu YC, Kjer-Nielsen L, Purcell AW, Burrows SR, McCluskey J, Rossjohn J
J Immunol 188 311-21 (2012)
PMID: 22140258

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero octamer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208597 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
T cell receptor alpha chain constant Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 203 amino acids
Theoretical weight: 22.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01848 (Residues: 1-93; Coverage: 66%)
Gene names: TCRA, TRAC
Sequence domains: Domain of unknown function (DUF1968)
Structure domains: Immunoglobulins
RL42 T cell receptor, beta chain Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 244 amino acids
Theoretical weight: 27.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P1
Unit cell:
a: 74.97Å b: 77.81Å c: 99.64Å
α: 69.35° β: 72.2° γ: 83.33°
R-values:
R R work R free
0.199 0.194 0.292
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

T cell antigen receptor recognition of antigen-presenting molecules.
Rossjohn et al. (2015)
10 more

1 mention without citation

Topology evaluation of models for difficult targets in the 14th round of the critical assessment of protein structure prediction (CASP14).
Kinch et al. (2021)