Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase (Q46Y89)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q46Y89
- Type
- protein
- Length
- 590 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- ATP-dependent lipid a-core flippase
- UniProt
- Q46Y89
- Pockets
- 5 · best druggability 0.63
Structure
1 distinct chain · 66% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent lipid a-core flippase | protein | 590 | 66% helix, 10% strand | Q46Y89 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.63 | 0.83 | 20 | empty |
| 2 | 511 | 0.60 | 0.74 | 47 | empty |
| 3 | 52 | 0.29 | 0.76 | 14 | empty |
| 4 | 54 | 0.28 | 0.74 | 11 | empty |
| 5 | 63 | 0.28 | 0.73 | 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 Q46Y89
- Elsewhere: UniProt Q46Y89 · AlphaFold DB Q46Y89
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