1LE4: Apolipoprotein E4

Name: PDB 1LE4: Structural basis for altered function in the common mutants of human apolipoprotein-E
Published: 1992-10-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: lipoprotein

Structural basis for altered function in the common mutants of human apolipoprotein-E. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Oct 1992.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,251
Mol. weight: 16.8 kDa
Released: 15 Oct 1992

Explore 1LE4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LE4 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

Element	Residues	Length
α-helix	25-42	18
α-helix	45-50	6
α-helix	55-78	24
α-helix	89-125	37
α-helix	131-160	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apolipoprotein E4	A	protein	144	Homo sapiens	P02649 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1LE4_1 APOLIPOPROTEIN E4 (chains A)
GQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQL
TPVAEETRARLSKELQAAQARLGADMEDVRGRLVQYRGEVQAMLGQSTEELRVRLASHLR
KLRKRLLRDADDLQKRLAVYQAGA

Primary citation

Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms. Dong, L.M., Wilson, C., Wardell, M.R. et al. J Biol Chem (1994) 269:22358-22365. PubMed

Other PDB entries of the same protein (UniProt P02649 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7FCR 1.4 Å, Crystal structure of the N-terminal domain of mutants of Human Apolipoprotein-E (ApoE)
8AX9 1.55 Å, Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P212121)
8AX8 1.55 Å, Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P3121)
7FCS 1.6 Å, Crystal structure of the N-terminal domain of mutants of Human Apolipoprotein-E (ApoE)
1GS9 1.7 Å, Apolipoprotein E4, 22k domain
6NCO 1.71 Å, Fragment-based Discovery of an apoE4 Stabilizer
1OR3 1.73 Å, Apolipoprotein E3 (APOE3), trigonal truncation mutant 165
8CE0 1.75 Å, N-terminal domain of human apolipoprotein E
1NFN 1.8 Å, Apolipoprotein E3 (APOE3)
6NCN 1.82 Å, Fragment-based Discovery of an apoE4 Stabilizer
1BZ4 1.85 Å, Apolipoprotein E3 (apo-E3), truncation mutant 165
9SA6 1.89 Å, Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P212121)

Browse structure collections

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