› 3low

X-ray diffraction
2.3Å resolution

Crystal structure of Beta 2 Microglobulin domain-swapped dimer

Released:
DOI: 10.2210/pdb3low/pdb
PDB entry 3low coloured by chain, front view.
PDB entry 3low coloured by chain, side view.
PDB entry 3low coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
Liu C, Sawaya MR, Eisenberg D
Nat Struct Mol Biol 18 49-55 (2011)
PMID: 21131979

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158376 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-2-microglobulin Chains: A, B
Molecule details ›
Chains: A, 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
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 59.721Å b: 29.162Å c: 67.715Å
α: 90° β: 97.49° γ: 90°
R-values:
R R work R free
0.222 0.219 0.266
Expression system: Escherichia coli

Quick links

Citations

14 review citations

A diversity of assembly mechanisms of a generic amyloid fold.
Eichner et al. (2011)
13 more

5 mentions without citation

The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.
Loureiro et al. (2020)
4 more