› 1oeh

Solution NMR

Human prion protein 61-68

Released:
DOI: 10.2210/pdb1oeh/pdb
PDB entry 1oeh coloured by chain, ensemble of 20 models, front view.
PDB entry 1oeh coloured by chain, ensemble of 20 models, side view.
PDB entry 1oeh coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site.
Zahn R
J Mol Biol 334 477-88 (2003)
PMID: 14623188

Function and Biology Details

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

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: 8 amino acids
Theoretical weight: 796 Da
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04156 (Residues: 77-84; Coverage: 4%)
Gene names: ALTPRP, PRIP, PRNP, PRP

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(DE3)

Quick links

Citations

13 review citations

The prion protein and lipid rafts.
Taylor et al. (2006)
12 more

5 mentions without citation

ProtDCal: A program to compute general-purpose-numerical descriptors for sequences and 3D-structures of proteins.
Ruiz-Blanco et al. (2015)
4 more