1lg4

Solution NMR

NMR structure of the human doppel protein fragment 24-152

Released:
Source organism: Homo sapiens
Primary publication:
NMR structure of the human doppel protein.
J Mol Biol 326 1549-57 (2003)
PMID: 12595265

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prion-like protein doppel Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UKY0 (Residues: 24-152; Coverage: 84%)
Gene names: DPL, PRND, UNQ1830/PRO3443
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
Chemical shifts: BMR5145  
Expression system: Escherichia coli BL21(DE3)