Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase (Q492S9)
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
- Q492S9
- Type
- protein
- Length
- 584 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x14De9B50550E2173e0C98fD70505d1A94f47f847
- Molecule
- ATP-dependent lipid a-core flippase
- UniProt
- Q492S9
- Pockets
- 6 · best druggability 0.58
Structure
1 distinct chain · 66% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent lipid a-core flippase | protein | 584 | 66% helix, 10% strand | Q492S9 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.58 | 0.77 | 37 | empty |
| 2 | 274 | 0.58 | 0.78 | 24 | empty |
| 3 | 111 | 0.52 | 0.81 | 26 | empty |
| 4 | 153 | 0.46 | 0.76 | 22 | empty |
| 5 | 82 | 0.45 | 0.80 | 19 | 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 Q492S9
- Elsewhere: UniProt Q492S9 · AlphaFold DB Q492S9
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