2YT1: PDB entry 2YT1

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.

Method
Solution NMR
Organism
Mus musculus
Chains
1
Atoms
1,396
Mol. weight
20.01 kDa
Released
8 Apr 2008

Explore 2YT1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YT1 contains 5 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.

Chain A: 5 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix13-2311
β-strand26-2721
α-helix29-357
β-strand71-82121
α-helix89-10214
α-helix1091
β-strand110-11671
β-strand119-12461
β-strand133-13641
β-strand142-14541
β-strand151-15771
β-strand163-17081
α-helix175-18410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2Aprotein185Mus musculusQ9DBR4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2YT1_1 Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2 (chains A)
GSSGSSGDAAVTPEERHLSKMQQNGYENPTYKFFEQMQNSGPSSGIEGRGSSGSSGSSGS
SGPTPKTELVQKFRVQYLGMLPVDRPVGMDTLNSAIENLMTSSSKEDWPSVNMNVADATV
TVISEKNEEEVLVECRVRFLSFMGVGKDVHTFAFIMDTGNQRFECHVFWCEPNAANVSEA
VQAAC

Primary citation

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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