Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease Y (Q03VG1)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease Y (Q03VG1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q03VG1
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa5bBccF395a3ABe9B629B9f9f8fBd173cC6F75b8
- Molecule
- Ribonuclease Y
- UniProt
- Q03VG1
- Pockets
- 4 · best druggability 0.47
Structure
1 distinct chain · 73% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease Y | protein | 518 | 73% helix, 7% strand | Q03VG1 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.47 | 0.83 | 14 | empty |
| 2 | 91 | 0.38 | 0.77 | 16 | empty |
| 3 | 63 | 0.31 | 0.75 | 15 | empty |
| 4 | 61 | 0.30 | 0.75 | 13 | 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 Q03VG1
- Elsewhere: UniProt Q03VG1 · AlphaFold DB Q03VG1
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