Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease Y (A6L227)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease Y (A6L227) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6L227
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Ribonuclease Y
- UniProt
- A6L227
- Pockets
- 5 · best druggability 0.47
Structure
1 distinct chain · 71% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease Y | protein | 511 | 71% helix, 7% strand | A6L227 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.47 | 0.82 | 15 | empty |
| 2 | 122 | 0.41 | 0.75 | 25 | empty |
| 3 | 95 | 0.36 | 0.75 | 17 | empty |
| 4 | 93 | 0.35 | 0.74 | 14 | empty |
| 5 | 71 | 0.32 | 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 A6L227
- Elsewhere: UniProt A6L227 · AlphaFold DB A6L227
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