1BZ4: Protein

Apolipoprotein E3 (apo-E3), truncation mutant 165. Determined by X-ray diffraction at 1.85 Å resolution. Released 11 Nov 1998.

Method
X-ray diffraction
Resolution
1.85 Å
Organism
Homo sapiens
Chains
1
Atoms
1,404
Mol. weight
16.76 kDa
Released
11 Nov 1998

Explore 1BZ4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BZ4 contains 6 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: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix25-4218
α-helix45-528
α-helix55-7824
α-helix82-843
α-helix87-12438
α-helix131-16131

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (apolipoprotein E)Aprotein144Homo sapiensP02649 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1BZ4_1 PROTEIN (APOLIPOPROTEIN E) (chains A)
SGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQ
LTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHL
RKLRKRLLRDADDLQKRLAVYQAG

Primary citation

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:

Browse structure collections

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