› 6tdo

X-ray diffraction
1.65Å resolution

Crystal structure of the disulfide engineered HLA-A0201 molecule in complex with one GM dipeptide in the A pocket.

Released:
DOI: 10.2210/pdb6tdo/pdb
PDB entry 6tdo coloured by chain, front view.
PDB entry 6tdo coloured by chain, side view.
PDB entry 6tdo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection.
Anjanappa R, Garcia-Alai M, Kopicki JD, Lockhauserbäumer J, Aboelmagd M, Hinrichs J, Nemtanu IM, Uetrecht C, Zacharias M, Springer S, Meijers R
Nat Commun 11 1314 (2020)
PMID: 32161266

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123614 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig-like domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 31.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: F6IQS1 (Residues: 24-299; Coverage: 88%)
Gene name: HLA-A
Sequence domains:
Beta-2-microglobulin Chain: B
Molecule details ›
Chain: B
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

Ligands and Environments

3 bound ligands:
Ligand GLY 1 x GLY
Ligand MET 1 x MET
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 52.936Å b: 80.914Å c: 56.351Å
α: 90° β: 112.74° γ: 90°
R-values:
R R work R free
0.188 0.186 0.224
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Dynamics of MHC-I molecules in the antigen processing and presentation pathway.
Truong et al. (2021)
5 more

1 mention without citation

Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection.
Anjanappa et al. (2020)