› 4w5p

X-ray diffraction
1.15Å resolution

Prp peptide

Released:
DOI: 10.2210/pdb4w5p/pdb
PDB entry 4w5p coloured by chain, front view.
PDB entry 4w5p coloured by chain, side view.
PDB entry 4w5p coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Crystal Structures of Polymorphic Prion Protein β1 Peptides Reveal Variable Steric Zipper Conformations.
Yu L, Lee SJ, Yee VC
Biochemistry 54 3640-8 (2015)
PMID: 25978088

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PrP peptide Chains: A, B
Molecule details ›
Chains: A, B
Length: 7 amino acids
Theoretical weight: 652 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 11.593Å b: 17.152Å c: 19.837Å
α: 90° β: 100.7° γ: 90°
R-values:
R R work R free
0.121 0.119 0.151
Expression system: Not provided

Quick links

Citations

1 review citation

Toward the Atomic Structure of PrPSc.
Rodriguez et al. (2017)
8 other articles

2 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
1 more