Solution structure of the tudor domain of the human smn protein. Determined by solution NMR. Released 2 May 2001.
Explore 1G5V in 3D Show helices and sheets RCSB PDB PDBe
1G5V contains 3 α-helices 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 | 133-137 | 5 | 1 |
| α-helix | 138-140 | 3 | |
| α-helix | 141 | 1 | |
| β-strand | 142 | 1 | 1 |
| α-helix | 143 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Survival motor neuron protein 1 | A | protein | 88 | Homo sapiens | Q16637 (AlphaFold model) |
>1G5V_1 SURVIVAL MOTOR NEURON PROTEIN 1 (chains A) KKNTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDL LSPICEVANNIEQNAQENENESQVSTDE
SMN tudor domain structure and its interaction with the Sm proteins. Selenko, P., Sprangers, R., Stier, G. et al. Nat Struct Biol (2001) 8:27-31. DOI 10.1038/83014 · 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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