High-resolution crystal structure of the E1-domain of the amyloid precursor protein. Determined by X-ray diffraction at 1.4 Å resolution. Released 4 Feb 2015.
Explore 4PWQ in 3D Show helices and sheets RCSB PDB PDBe
4PWQ contains 9 α-helices and 24 β-strands across 2 chains. 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 |
|---|---|---|---|
| β-strand | 33-35 | 3 | 4 |
| α-helix | 41-42 | 2 | |
| β-strand | 43-45 | 3 | 4 |
| β-strand | 52-54 | 3 | 4 |
| α-helix | 66-76 | 11 | |
| β-strand | 82-87 | 6 | 4 |
| β-strand | 92-94 | 3 | 5 |
| α-helix | 97-98 | 2 | |
| β-strand | 99 | 1 | 6 |
| β-strand | 103 | 1 | 6 |
| β-strand | 110-112 | 3 | 5 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 4 |
| β-strand | 134-139 | 6 | 7 |
| β-strand | 145-146 | 2 | 7 |
| α-helix | 147-159 | 13 | |
| β-strand | 163-175 | 13 | 7 |
| β-strand | 178-188 | 11 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 33-35 | 3 | 1 |
| α-helix | 41-42 | 2 | |
| β-strand | 43-46 | 4 | 1 |
| β-strand | 51-54 | 4 | 1 |
| α-helix | 55 | 1 | |
| α-helix | 66-76 | 11 | |
| β-strand | 82-87 | 6 | 1 |
| β-strand | 92-94 | 3 | 2 |
| β-strand | 110-112 | 3 | 2 |
| β-strand | 115-119 | 5 | 1 |
| β-strand | 134-139 | 6 | 3 |
| β-strand | 145-146 | 2 | 3 |
| α-helix | 147-160 | 14 | |
| β-strand | 163-175 | 13 | 3 |
| β-strand | 178-188 | 11 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amyloid beta A4 protein | A, B | protein | 191 | Homo sapiens | P05067 (AlphaFold model) |
>4PWQ_1 Amyloid beta A4 protein (chains A, B) MLEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEV YPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFL HQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAIEGRKL AAALEHHHHHH
The Amyloid Precursor Protein Shows a pH-Dependent Conformational Switch in Its E1 Domain. Hoefgen, S., Dahms, S.O., Oertwig, K. et al. J Mol Biol (2015) 427:433-442. DOI 10.1016/j.jmb.2014.12.005 · PubMed
Other PDB entries of the same protein (UniProt P05067 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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