Structure analysis

Probing the N-terminal beta-sheet conversion in the crystal structure of the full-length human prion protein bound to a Nanobody

X-ray diffraction
1.5Å resolution
Source organisms:
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 11531.39 Å2
Buried surface area: 1257.48 Å2
Dissociation area: 628.74 Å2
Dissociation energy (ΔGdiss): -2.85 kcal/mol
Dissociation entropy (TΔSdiss): 10.91 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-208987

Macromolecules

Chain: A
Length: 241 amino acids
Theoretical weight: 26.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 24-231; Coverage: 90%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Pfam: Prion/Doppel alpha-helical domain
InterPro:

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Chain: B
Length: 130 amino acids
Theoretical weight: 14.28 KDa
Source organism: Lama glama
Expression system: Escherichia coli
InterPro:
CATH: Immunoglobulins

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