Research workbench
Solution structure of smn tudor domain in complex with asymmetrically dimethylated arginine
Analyse Solution structure of smn tudor domain in complex with asymmetrically… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A4G
- Type
- protein
- Length
- 64 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Survival motor neuron protein
- UniProt
- Q16637
- Ligands
- DA2
Structure
solution nmr · 1 distinct chain · 0% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Survival motor neuron protein | protein | 64 | 0% helix, 42% strand | Q16637 |
Ligands and binding sites
- DA2 · Ng,ng-dimethyl-L-arginine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4A4G · Solution structure of SMN Tudor domain in complex with asymmetrically dimethylated… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16637 · AlphaFold monomer V2.0 prediction for survival motor neuron protein (Q16637) · a predicted model of the same protein · chain A against A, TM-score 0.88
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q16637
- Elsewhere: RCSB PDB 4A4G · PDBe 4A4G · UniProt Q16637
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