Research workbench
AlphaFold monomer V2.0 prediction for rhophilin-2 (A4FUC9)
Analyse AlphaFold monomer V2.0 prediction for rhophilin-2 (A4FUC9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4FUC9
- Type
- protein
- Length
- 686 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Rhophilin-2
- UniProt
- A4FUC9
- Pockets
- 9 · best druggability 0.69
Structure
1 distinct chain · 49% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhophilin-2 | protein | 686 | 49% helix, 6% strand | A4FUC9 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 665 | 0.69 | 0.77 | 78 | empty |
| 2 | 200 | 0.61 | 0.82 | 20 | empty |
| 3 | 422 | 0.61 | 0.76 | 58 | empty |
| 4 | 99 | 0.42 | 0.78 | 23 | empty |
| 5 | 62 | 0.37 | 0.79 | 14 | 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 A4FUC9
- Elsewhere: UniProt A4FUC9 · AlphaFold DB A4FUC9
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