Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase (Q3IGX5)
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
- Q3IGX5
- Type
- protein
- Length
- 581 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd9004EA8bb29b982431948B179095C248197194f
- Molecule
- ATP-dependent lipid a-core flippase
- UniProt
- Q3IGX5
- Pockets
- 7 · 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 | 581 | 66% helix, 10% strand | Q3IGX5 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.58 | 0.75 | 45 | empty |
| 2 | 133 | 0.56 | 0.82 | 22 | empty |
| 3 | 126 | 0.46 | 0.77 | 19 | empty |
| 4 | 62 | 0.45 | 0.83 | 16 | empty |
| 5 | 67 | 0.39 | 0.79 | 18 | 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 Q3IGX5
- Elsewhere: UniProt Q3IGX5 · AlphaFold DB Q3IGX5
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