Research workbench
AlphaFold monomer V2.0 prediction for UPF0246 protein FMG_1068 (B0S296)
Analyse AlphaFold monomer V2.0 prediction for UPF0246 protein FMG_1068 (B0S296) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0S296
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- UPF0246 protein FMG_1068
- UniProt
- B0S296
- Pockets
- 3 · best druggability 0.47
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0246 protein FMG_1068 | protein | 244 | 43% helix, 22% strand | B0S296 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.47 | 0.77 | 26 | empty |
| 2 | 119 | 0.47 | 0.79 | 20 | empty |
| 3 | 57 | 0.37 | 0.80 | 12 | 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 B0S296
- Elsewhere: UniProt B0S296 · AlphaFold DB B0S296
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