Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease Y (B1LAG5)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease Y (B1LAG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1LAG5
- Type
- protein
- Length
- 507 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Ribonuclease Y
- UniProt
- B1LAG5
- Pockets
- 4 · best druggability 0.51
Structure
1 distinct chain · 72% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease Y | protein | 507 | 72% helix, 7% strand | B1LAG5 |
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 | 68 | 0.51 | 0.85 | 16 | empty |
| 2 | 200 | 0.43 | 0.73 | 33 | empty |
| 3 | 76 | 0.38 | 0.78 | 13 | empty |
| 4 | 54 | 0.28 | 0.74 | 10 | 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 B1LAG5
- Elsewhere: UniProt B1LAG5 · AlphaFold DB B1LAG5
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