Structure of human FE65-WW domain in complex with hMena peptide. Determined by X-ray diffraction at 1.33 Å resolution. Released 10 Jul 2007.
Explore 2HO2 in 3D Show helices and sheets RCSB PDB PDBe
2HO2 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 | 259-263 | 5 | 1 |
| β-strand | 268-272 | 5 | 1 |
| β-strand | 277-279 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-9 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amyloid beta A4 protein-binding family B member 1 | A | protein | 38 | Homo sapiens | O00213 (AlphaFold model) |
| Protein enabled homolog | B | protein | 10 | Q8N8S7 (AlphaFold model) |
>2HO2_1 Amyloid beta A4 protein-binding family B member 1 (chains A) GSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPS
>2HO2_2 Protein enabled homolog (chains B) PPPPPPPPPL
Structural Basis for Polyproline Recognition by the FE65 WW Domain. Meiyappan, M., Birrane, G., Ladias, J.A. J Mol Biol (2007) 372:970-980. DOI 10.1016/j.jmb.2007.06.064 · PubMed
Other PDB entries of the same protein (UniProt O00213 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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