4kml

X-ray diffraction
1.5Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-208987 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Major prion protein Chain: A
Molecule details ›
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
Sequence domains: Prion/Doppel alpha-helical domain
Nanobody Chain: B
Molecule details ›
Chain: B
Length: 130 amino acids
Theoretical weight: 14.28 KDa
Source organism: Lama glama
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 131.442Å b: 45.921Å c: 44.964Å
α: 90° β: 96.09° γ: 90°
R-values:
R R work R free
0.176 0.175 0.192
Expression system: Escherichia coli