› 3o79

X-ray diffraction
1.6Å resolution

Crystal Structure of Wild-type Rabbit PrP 126-230

Released:
DOI: 10.2210/pdb3o79/pdb
PDB entry 3o79 coloured by chain, front view.
PDB entry 3o79 coloured by chain, side view.
PDB entry 3o79 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP.
Khan MQ, Sweeting B, Mulligan VK, Arslan PE, Cashman NR, Pai EF, Chakrabartty A
Proc Natl Acad Sci U S A 107 19808-13 (2010)
PMID: 21041683

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 105 amino acids
Theoretical weight: 12.44 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9TSF8 (Residues: 127-231; Coverage: 44%)
Gene name: PrP
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

3 bound ligands:
Ligand NA 4 x NA
Ligand CL 2 x CL
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 29.53Å b: 86.17Å c: 87.14Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.157 0.218
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.
Nagel-Steger et al. (2016)
15 more

7 mentions without citation

Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP.
Khan et al. (2010)
6 more