Apolipoprotein E3 (APOE3). Determined by X-ray diffraction at 1.8 Å resolution. Released 27 Jan 1997.
Explore 1NFN in 3D Show helices and sheets RCSB PDB PDBe
1NFN 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 | 25-42 | 18 | |
| α-helix | 45-51 | 7 | |
| α-helix | 55-78 | 24 | |
| α-helix | 93-124 | 32 | |
| α-helix | 131-162 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apolipoprotein E3 | A | protein | 191 | Homo sapiens | P02649 (AlphaFold model) |
>1NFN_1 APOLIPOPROTEIN E3 (chains A) KVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQEL RALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRG EVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRER LGPLVEQGRVR
Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. Dong, L.M., Parkin, S., Trakhanov, S.D. et al. Nat Struct Biol (1996) 3:718-722. DOI 10.1038/nsb0896-718 · 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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