Research workbench
AlphaFold monomer V2.0 prediction for protein nipsnap homolog 3A (Q5RAA9)
Analyse AlphaFold monomer V2.0 prediction for protein nipsnap homolog 3A (Q5RAA9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RAA9
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Protein nipsnap homolog 3A
- UniProt
- Q5RAA9
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein nipsnap homolog 3A | protein | 247 | 35% helix, 31% strand | Q5RAA9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.64 | 0.86 | 24 | empty |
| 2 | 108 | 0.53 | 0.83 | 23 | empty |
| 3 | 88 | 0.49 | 0.82 | 20 | empty |
| 4 | 60 | 0.38 | 0.79 | 21 | empty |
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 Q5RAA9
- Elsewhere: UniProt Q5RAA9 · AlphaFold DB Q5RAA9
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