› 1odp

Solution NMR

PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.6, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40

Released:
DOI: 10.2210/pdb1odp/pdb
PDB entry 1odp coloured by chain, ensemble of 5 models, front view.
PDB entry 1odp coloured by chain, ensemble of 5 models, side view.
PDB entry 1odp coloured by chain, ensemble of 5 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions.
Wang G, Treleaven WD, Cushley RJ
Biochim Biophys Acta 1301 174-84 (1996)
PMID: 8664326

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-135984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Truncated apolipoprotein A-I Chain: A
Molecule details ›
Chain: A
Length: 20 amino acids
Theoretical weight: 2.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02647 (Residues: 190-209; Coverage: 8%)
Gene name: APOA1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

9 review citations

Structural models of human apolipoprotein A-I: a critical analysis and review.
Brouillette et al. (2001)
8 more

3 mentions without citation

Generalized pattern search algorithm for Peptide structure prediction.
Nicosia et al. (2008)
2 more