Research workbench
AlphaFold monomer V2.0 prediction for probable ribonuclease fau-1 (Q5V0I9)
Analyse AlphaFold monomer V2.0 prediction for probable ribonuclease fau-1 (Q5V0I9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5V0I9
- Type
- protein
- Length
- 466 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Probable ribonuclease fau-1
- UniProt
- Q5V0I9
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable ribonuclease fau-1 | protein | 466 | 28% helix, 32% strand | Q5V0I9 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 287 | 0.64 | 0.81 | 47 | empty |
| 2 | 144 | 0.46 | 0.77 | 20 | empty |
| 3 | 92 | 0.35 | 0.74 | 18 | 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 Q5V0I9
- Elsewhere: UniProt Q5V0I9 · AlphaFold DB Q5V0I9
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