Solution structure of SMN Tudor domain in complex with asymmetrically dimethylated arginine. Determined by solution NMR. Released 30 Nov 2011.
Explore 4A4G in 3D Show helices and sheets RCSB PDB PDBe
4A4G contains 0 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 |
| β-strand | 142 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Survival motor neuron protein | A | protein | 64 | HOMO SAPIENS | Q16637 (AlphaFold model) |
>4A4G_1 SURVIVAL MOTOR NEURON PROTEIN (chains A) NTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLS PICE
| ID | Name | Formula | Copies |
|---|---|---|---|
| DA2 | Ng,ng-dimethyl-L-arginine | C8 H18 N4 O2 | 1 |
Structural Basis for Dimethyl-Arginine Recognition by the Tudor Domains of Human Smn and Spf30 Proteins. Tripsianes, K., Madl, T., Machyna, M. et al. Nat Struct Mol Biol (2011) 18:1414. DOI 10.1038/NSMB.2185 · 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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