2DYF: First WW domain of FBP11 / HYPA

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.

Method
Solution NMR
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
2
Atoms
317
Mol. weight
4.51 kDa
Released
24 Oct 2006

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

Secondary structure: helices and β-sheets

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.

Chain A: 0 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand12-1651
β-strand22-2651
β-strand31-3331
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix5-84

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Huntingtin-interacting protein HYPA/FBP11Aprotein30Homo sapiensO75400 (AlphaFold model)
PL (PPLP) motif peptide from Myosin tail region-interacting protein MTI1Bprotein9Saccharomyces cerevisiaeP47068 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2DYF_1 Huntingtin-interacting protein HYPA/FBP11 (chains A)
GSWTEHKSPDGRTYYYNTETKQSTWEKPDD
Sequence of entity 2 (B), FASTA
>2DYF_2 PL (PPLP) motif peptide from Myosin tail region-interacting protein MTI1 (chains B)
GSTAPPLPR

Primary citation

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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