Apolipoprotein E3 (APOE3), trigonal truncation mutant 165. Determined by X-ray diffraction at 1.73 Å resolution. Released 24 May 2000.
Explore 1OR3 in 3D Show helices and sheets RCSB PDB PDBe
1OR3 contains 5 α-helices 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 | 25-41 | 17 | |
| α-helix | 45-52 | 8 | |
| α-helix | 55-81 | 27 | |
| α-helix | 92-122 | 31 | |
| α-helix | 131-162 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (apolipoprotein E) | A | protein | 165 | Homo sapiens | P02649 (AlphaFold model) |
>1OR3_1 PROTEIN (APOLIPOPROTEIN E) (chains A) KVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQEL RALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRG EVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAG
Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding. Segelke, B.W., Forstner, M., Knapp, M. et al. Protein Sci (2000) 9:886-897. PubMed
Other PDB entries of the same protein (UniProt P02649 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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