Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L. Determined by solution NMR. Released 8 Apr 2008.
Explore 2YT0 in 3D Show helices and sheets RCSB PDB PDBe
2YT0 contains 6 α-helices and 8 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 | 13-23 | 11 | |
| β-strand | 26-27 | 2 | 1 |
| α-helix | 30-33 | 4 | |
| β-strand | 63-73 | 11 | 1 |
| α-helix | 80-93 | 14 | |
| α-helix | 100 | 1 | |
| β-strand | 101-105 | 5 | 1 |
| α-helix | 107-109 | 3 | |
| β-strand | 110-115 | 6 | 1 |
| β-strand | 122-127 | 6 | 1 |
| β-strand | 133-136 | 4 | 1 |
| β-strand | 142-150 | 9 | 1 |
| β-strand | 153-161 | 9 | 1 |
| α-helix | 166-175 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2 | A | protein | 176 | Mus musculus | Q9DBR4 (AlphaFold model) |
>2YT0_1 Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2 (chains A) GSSGSSGDAAVTPEERHLSKMQQNGYENPTYKFFEQMQNSGSSGSSGSSGSSGPTPKTEL VQKFRVQYLGMLPVDRPVGMDTLNSAIENLMTSSSKEDWPSVNMNVADATVTVISEKNEE EVLVECRVRFLSFMGVGKDVHTFAFIMDTGNQRFECHVFWCEPNAANVSEAVQAAC
Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode. Li, H., Koshiba, S., Hayashi, F. et al. J Biol Chem (2008) 283:27165-27178. DOI 10.1074/jbc.M803892200 · PubMed
Other PDB entries of the same protein (UniProt Q9DBR4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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