1NFO: Apolipoprotein E2

Apolipoprotein E2 (APOE2, D154A mutation). Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Jan 1997.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,216
Mol. weight
22.06 kDa
Released
27 Jan 1997

Explore 1NFO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NFO 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.

Chain A: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix25-4218
α-helix45-528
α-helix55-7824
α-helix93-12432
α-helix131-16030

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apolipoprotein E2Aprotein191Homo sapiensP02649 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1NFO_1 APOLIPOPROTEIN E2 (chains A)
KVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQEL
RALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRG
EVQAMLGQSTEELRVRLASHLRKLRKRLLRDADALQKCLAVYQAGAREGAERGLSAIRER
LGPLVEQGRVR

Primary citation

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:

Browse structure collections

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