High resolution crystal structure of the SMN Tudor domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 25 Mar 2003.
Explore 1MHN in 3D Show helices and sheets RCSB PDB PDBe
1MHN contains 1 α-helix and 5 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 |
|---|---|---|---|
| β-strand | 97-101 | 5 | 1 |
| β-strand | 108-117 | 10 | 1 |
| β-strand | 122-127 | 6 | 1 |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 138-140 | 3 | |
| β-strand | 142 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Survival motor neuron protein | A | protein | 59 | Homo sapiens | Q16637 (AlphaFold model) |
>1MHN_1 Survival motor neuron protein (chains A) LQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICE
High Resolution X-ray and NMR Structures of the SMN Tudor Domain: conformational variation in the binding site for symmetrically dimethylated arginine residues. Sprangers, R., Groves, M.R., Sinning, I. et al. J Mol Biol (2003) 327:507-520. DOI 10.1016/S0022-2836(03)00148-7 · PubMed
Other PDB entries of the same protein (UniProt Q16637 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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