1xu0

Solution NMR

Solution structure of Xenopus leavis prion protein

Released:
Source organism: Xenopus laevis
Primary publication:
Prion protein NMR structures of chickens, turtles, and frogs.
Proc Natl Acad Sci U S A 102 651-5 (2005)
PMID: 15647366

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-177797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prion/Doppel protein beta-ribbon domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 15.02 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q5S1W7 (Residues: 43-171; Coverage: 75%)
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21