Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase (Q1CGH0)
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
- Q1CGH0
- Type
- protein
- Length
- 582 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- ATP-dependent lipid a-core flippase
- UniProt
- Q1CGH0
- Pockets
- 7 · best druggability 0.59
Structure
1 distinct chain · 66% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent lipid a-core flippase | protein | 582 | 66% helix, 10% strand | Q1CGH0 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 378 | 0.59 | 0.76 | 34 | empty |
| 2 | 80 | 0.55 | 0.86 | 21 | empty |
| 3 | 88 | 0.51 | 0.83 | 18 | empty |
| 4 | 137 | 0.42 | 0.75 | 23 | empty |
| 5 | 52 | 0.32 | 0.77 | 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 Q1CGH0
- Elsewhere: UniProt Q1CGH0 · AlphaFold DB Q1CGH0
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