Research workbench
AlphaFold monomer V2.0 prediction for antigenic heat-stable 120 kda protein (Q9AJ80)
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
- Q9AJ80
- Type
- protein
- Length
- 1,012 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5204FDdEa2155a2E5E05Dfb42AEbb4D8c9343AF1
- Molecule
- Antigenic heat-stable 120 kda protein
- UniProt
- Q9AJ80
- Pockets
- 7 · best druggability 0.56
Structure
1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antigenic heat-stable 120 kda protein | protein | 1012 | 56% helix, 9% strand | Q9AJ80 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.56 | 0.83 | 31 | empty |
| 2 | 136 | 0.50 | 0.79 | 20 | empty |
| 3 | 114 | 0.44 | 0.78 | 19 | empty |
| 4 | 96 | 0.43 | 0.79 | 21 | empty |
| 5 | 128 | 0.39 | 0.74 | 13 | 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 Q9AJ80
- Elsewhere: UniProt Q9AJ80 · AlphaFold DB Q9AJ80
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