Research workbench
AlphaFold monomer V2.0 prediction for AFG1-like ATPase (Q3V384)
Analyse AlphaFold monomer V2.0 prediction for AFG1-like ATPase (Q3V384) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3V384
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0f2d00ae1CFf3AeaF45a8e479E79034189a58EdD
- Molecule
- AFG1-like ATPase
- UniProt
- Q3V384
- Pockets
- 6 · best druggability 0.82
Structure
1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AFG1-like ATPase | protein | 480 | 45% helix, 14% strand | Q3V384 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1051 | 0.82 | 0.83 | 88 | empty |
| 2 | 85 | 0.56 | 0.86 | 19 | empty |
| 3 | 110 | 0.40 | 0.76 | 23 | empty |
| 4 | 65 | 0.29 | 0.74 | 14 | empty |
| 5 | 54 | 0.26 | 0.73 | 14 | 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 Q3V384
- Elsewhere: UniProt Q3V384 · AlphaFold DB Q3V384
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