› 3hak

X-ray diffraction
1.8Å resolution

Human prion protein variant V129

Released:
DOI: 10.2210/pdb3hak/pdb
PDB entry 3hak coloured by chain, front view.
PDB entry 3hak coloured by chain, side view.
PDB entry 3hak coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC
EMBO J 29 251-62 (2010)
PMID: 19927125

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 12.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 125-227; Coverage: 45%)
Gene names: ALTPRP, PRIP, PRNP, PRP
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
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 32.484Å b: 49.091Å c: 56.885Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.241
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Molecular biology and pathology of prion strains in sporadic human prion diseases.
Gambetti et al. (2011)
7 more

11 mentions without citation

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Lee et al. (2010)
10 more