Peptide of human apoa-I residues 166-185. NMR, 5 structures at PH 6.0, 37 degrees celsius and peptide:dpc mole ratio of 1:40. Determined by solution NMR. Released 10 Jun 1996.
Explore 1ODR in 3D Show helices and sheets RCSB PDB PDBe
1ODR contains 1 α-helix and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-16 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoa-I peptide | A | protein | 20 | Homo sapiens | P02647 (AlphaFold model) |
>1ODR_1 APOA-I PEPTIDE (chains A) YSDELRQRLAARLEALKENG
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, W.D., Cushley, R.J. Biochim Biophys Acta (1996) 1301:174-184. DOI 10.1016/0005-2760(96)00037-9 · PubMed
Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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