› 3sgo

X-ray diffraction
2.56Å resolution

Amyloid-related segment of alphaB-crystallin residues 90-100

Released:
DOI: 10.2210/pdb3sgo/pdb
PDB entry 3sgo coloured by chain, front view.
PDB entry 3sgo coloured by chain, side view.
PDB entry 3sgo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Atomic view of a toxic amyloid small oligomer.
Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D
Science 335 1228-31 (2012)
PMID: 22403391

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135880 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-crystallin B chain Chain: A
Molecule details ›
Chain: A
Length: 11 amino acids
Theoretical weight: 1.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02511 (Residues: 90-100; Coverage: 6%)
Gene names: CRYA2, CRYAB, HSPB5

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I4132
Unit cell:
a: 69.284Å b: 69.284Å c: 69.284Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.244 0.27
Expression system: Not provided

Quick links

Citations

68 review citations

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases.
Jucker et al. (2013)
67 more

11 mentions without citation

Amyloid polymorphism: structural basis and neurobiological relevance.
Tycko R. (2015)
10 more