Research workbench
AlphaFold monomer V2.0 prediction for zinc finger ccch-type antiviral protein 1-like (Q96H79)
Analyse AlphaFold monomer V2.0 prediction for zinc finger ccch-type antiviral protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96H79
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Zinc finger ccch-type antiviral protein 1-like
- UniProt
- Q96H79
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 36% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger ccch-type antiviral protein 1-like | protein | 300 | 36% helix, 8% strand | Q96H79 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.41 | 0.80 | 17 | empty |
| 2 | 94 | 0.39 | 0.76 | 15 | empty |
| 3 | 55 | 0.29 | 0.74 | 11 | empty |
| 4 | 59 | 0.28 | 0.74 | 17 | 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 Q96H79
- Elsewhere: UniProt Q96H79 · AlphaFold DB Q96H79
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