Research workbench
AlphaFold monomer V2.0 prediction for antigenic heat-stable 120 kda protein (Q9AJ81)
Analyse AlphaFold monomer V2.0 prediction for antigenic heat-stable 120 kda protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9AJ81
- Type
- protein
- Length
- 1,013 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a7b1782CE62A880494cB63CE2416dfA7aC6391d
- Molecule
- Antigenic heat-stable 120 kda protein
- UniProt
- Q9AJ81
- Pockets
- 6 · best druggability 0.63
Structure
1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antigenic heat-stable 120 kda protein | protein | 1013 | 56% helix, 9% strand | Q9AJ81 |
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 | 711 | 0.63 | 0.73 | 59 | empty |
| 2 | 244 | 0.62 | 0.81 | 46 | empty |
| 3 | 318 | 0.55 | 0.75 | 35 | empty |
| 4 | 143 | 0.49 | 0.78 | 22 | empty |
| 5 | 120 | 0.40 | 0.75 | 22 | 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 Q9AJ81
- Elsewhere: UniProt Q9AJ81 · AlphaFold DB Q9AJ81
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