› 6pq5

X-ray diffraction
1.5Å resolution

AGAAAA segment 113-118 from human prion

Released:
DOI: 10.2210/pdb6pq5/pdb
PDB 6pq5 coloured by chain and viewed from the front.
PDB 6pq5 coloured by chain and viewed from the side.
PDB 6pq5 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core.
Glynn C, Sawaya MR, Ge P, Gallagher-Jones M, Short CW, Bowman R, Apostol M, Zhou ZH, Eisenberg DS, Rodriguez JA
Nat. Struct. Mol. Biol. (2020)
PMID: 32284600

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 6 amino acids
Theoretical weight: 430 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04156 (Residues: 113-118; Coverage: 3%)
Gene names: ALTPRP, PRIP, PRNP, PRP

Ligands and Environments

1 bound ligand:
Ligand MLI 2 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P21
Unit cell:
a: 18.533Å b: 9.508Å c: 17.632Å
α: 90° β: 120.54° γ: 90°
R-values:
R R work R free
0.237 0.234 0.271
Expression system: Not provided

Quick links

Citations

6 review citations

Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition.
Subedi et al. (2022)
5 more