Apolipoprotein E4 (APOE4), 22K fragment. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Jul 2001.
Explore 1B68 in 3D Show helices and sheets RCSB PDB PDBe
1B68 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 | 45-51 | 7 | |
| α-helix | 55-78 | 24 | |
| α-helix | 87-124 | 38 | |
| α-helix | 131-161 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apolipoprotein E | A | protein | 191 | Homo sapiens | P02649 (AlphaFold model) |
>1B68_1 APOLIPOPROTEIN E (chains A) KVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQEL RALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVRGRLVQYRG EVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRER LGPLVEQGRVR
Interaction of the N-terminal domain of apolipoprotein E4 with heparin. Dong, J., Peters-Libeu, C.A., Weisgraber, K.H. et al. Biochemistry (2001) 40:2826-2834. DOI 10.1021/bi002417n · 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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