Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease 3 (F2NV13)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease 3 (F2NV13) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F2NV13
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Ribonuclease 3
- UniProt
- F2NV13
- Pockets
- 4 · best druggability 0.49
Structure
1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease 3 | protein | 369 | 52% helix, 14% strand | F2NV13 |
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 | 231 | 0.49 | 0.74 | 25 | empty |
| 2 | 112 | 0.41 | 0.76 | 20 | empty |
| 3 | 93 | 0.38 | 0.76 | 20 | empty |
| 4 | 67 | 0.28 | 0.73 | 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 F2NV13
- Elsewhere: UniProt F2NV13 · AlphaFold DB F2NV13
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