Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease Y (A9KMU8)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease Y (A9KMU8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9KMU8
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Ribonuclease Y
- UniProt
- A9KMU8
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 73% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease Y | protein | 516 | 73% helix, 7% strand | A9KMU8 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.50 | 0.83 | 16 | empty |
| 2 | 58 | 0.44 | 0.83 | 15 | empty |
| 3 | 53 | 0.42 | 0.83 | 13 | empty |
| 4 | 107 | 0.40 | 0.76 | 16 | 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 A9KMU8
- Elsewhere: UniProt A9KMU8 · AlphaFold DB A9KMU8
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