Structure analysis

Mouse prion protein (121-231) containing the substitution Y169A

Solution NMR
Source organism: Mus musculus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7325.19 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138267

Macromolecules

Chain: A
Length: 114 amino acids
Theoretical weight: 13.32 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04925 (Residues: 120-231; Coverage: 48%)
Gene names: Prn-p, Prnp, Prp
Pfam: Prion/Doppel alpha-helical domain
InterPro:
CATH: Prion/Doppel protein, beta-ribbon domain

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