RBM5 OCRE domain. Determined by solution NMR. Released 7 Dec 2016.
Explore 5MFY in 3D Show helices and sheets RCSB PDB PDBe
5MFY contains 1 α-helix and 6 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 | 12-14 | 3 | |
| β-strand | 16-18 | 3 | 1 |
| β-strand | 23-26 | 4 | 1 |
| β-strand | 31-33 | 3 | 1 |
| β-strand | 40-42 | 3 | 1 |
| β-strand | 47-52 | 6 | 1 |
| β-strand | 57-60 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-binding protein 5 | A | protein | 64 | Homo sapiens | P52756 (AlphaFold model) |
>5MFY_1 RNA-binding protein 5 (chains A) GAMGTKYAVPDTSTYQYDESSGYYYDPTTGLYYDPNSQYYYNSLTQQYLYWDGEKETYVP AAES
Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation. Mourao, A., Bonnal, S., Soni, K. et al. Elife (2016) 5. DOI 10.7554/eLife.14707 · PubMed
Other PDB entries of the same protein (UniProt P52756 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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