Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase (Q2LVL0)
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
- Q2LVL0
- Type
- protein
- Length
- 601 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- ATP-dependent lipid a-core flippase
- UniProt
- Q2LVL0
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 66% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent lipid a-core flippase | protein | 601 | 66% helix, 11% strand | Q2LVL0 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 307 | 0.64 | 0.80 | 38 | empty |
| 2 | 422 | 0.60 | 0.75 | 37 | empty |
| 3 | 81 | 0.51 | 0.83 | 18 | empty |
| 4 | 53 | 0.35 | 0.78 | 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 Q2LVL0
- Elsewhere: UniProt Q2LVL0 · AlphaFold DB Q2LVL0
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