› 3pdo

X-ray diffraction
1.95Å resolution

Crystal Structure of HLA-DR1 with CLIP102-120

Released:
DOI: 10.2210/pdb3pdo/pdb
PDB entry 3pdo coloured by chain, front view.
PDB entry 3pdo coloured by chain, side view.
PDB entry 3pdo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Bidirectional binding of invariant chain peptides to an MHC class II molecule.
Günther S, Schlundt A, Sticht J, Roske Y, Heinemann U, Wiesmüller KH, Jung G, Falk K, Rötzschke O, Freund C
Proc Natl Acad Sci U S A 107 22219-24 (2010)
PMID: 21115828

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-135318 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HLA class II histocompatibility antigen, DR alpha chain Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 22.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01903 (Residues: 26-217; Coverage: 84%)
Gene names: HLA-DRA, HLA-DRA1
Sequence domains:
Structure domains:
HLA class II histocompatibility antigen, DRB1 beta chain Chain: B
Molecule details ›
Chain: B
Length: 199 amino acids
Theoretical weight: 23.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01911 (Residues: 30-227; Coverage: 84%)
Gene name: HLA-DRB1
Sequence domains:
Structure domains:
Class-II-associated invariant chain peptide Chain: C
Molecule details ›
Chain: C
Length: 19 amino acids
Theoretical weight: 2.15 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04233 (Residues: 102-120; Coverage: 6%)
Gene names: CD74, DHLAG

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 45.45Å b: 97.627Å c: 99.052Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.24
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation.
Wieczorek et al. (2017)
6 more

37 mentions without citation

Conformational variation in structures of classical and non-classical MHCII proteins and functional implications.
Painter et al. (2012)
36 more