Research workbench
AlphaFold monomer V2.0 prediction for UPF0259 membrane protein BBP_256 (Q89AL2)
Analyse AlphaFold monomer V2.0 prediction for UPF0259 membrane protein BBP_256 (Q89AL2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q89AL2
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA35a3d2F3CD94d1eAB5DE310bC45150DB5ad0e80
- Molecule
- UPF0259 membrane protein BBP_256
- UniProt
- Q89AL2
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0259 membrane protein BBP_256 | protein | 250 | 83% helix, 0% strand | Q89AL2 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.76 | 0.84 | 38 | empty |
| 2 | 277 | 0.55 | 0.76 | 26 | empty |
| 3 | 73 | 0.42 | 0.79 | 13 | empty |
| 4 | 55 | 0.27 | 0.74 | 15 | 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 Q89AL2
- Elsewhere: UniProt Q89AL2 · AlphaFold DB Q89AL2
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