Research workbench
Solution structure of the tudor domain of the human smn protein
Analyse Solution structure of the tudor domain of the human smn protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G5V
- Type
- protein
- Length
- 56 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Survival motor neuron protein 1
- UniProt
- Q16637
Structure
solution nmr · 1 distinct chain · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Survival motor neuron protein 1 | protein | 56 | 5% helix, 48% strand | Q16637 |
Compared structures
- 1G5V · Solution structure of the tudor domain of the human smn protein · 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 0.94
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 1G5V · PDBe 1G5V · UniProt Q16637
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