Solution structure of the first WW domain of FBP11 / HYPA (FBP11 WW1) complexed with a PL (PPLP) motif peptide ligand. Determined by solution NMR. Released 24 Oct 2006.
Explore 2DYF in 3D Show helices and sheets RCSB PDB PDBe
2DYF contains 1 α-helix and 3 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 | 12-16 | 5 | 1 |
| β-strand | 22-26 | 5 | 1 |
| β-strand | 31-33 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-8 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Huntingtin-interacting protein HYPA/FBP11 | A | protein | 30 | Homo sapiens | O75400 (AlphaFold model) |
| PL (PPLP) motif peptide from Myosin tail region-interacting protein MTI1 | B | protein | 9 | Saccharomyces cerevisiae | P47068 (AlphaFold model) |
>2DYF_1 Huntingtin-interacting protein HYPA/FBP11 (chains A) GSWTEHKSPDGRTYYYNTETKQSTWEKPDD
>2DYF_2 PL (PPLP) motif peptide from Myosin tail region-interacting protein MTI1 (chains B) GSTAPPLPR
Complex structure of fbp11 ww1 and a pl ligand reveals the mechanism of proline-rich ligand recognition by group-II/III ww domains. Kato, Y., Miyakawa, T., Kurita, J. et al. To be published.
Other PDB entries of the same protein (UniProt O75400 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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