Research workbench
AlphaFold monomer V2.0 prediction for pup--protein ligase (A0QFB7)
Analyse AlphaFold monomer V2.0 prediction for pup--protein ligase (A0QFB7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0QFB7
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Pup--protein ligase
- UniProt
- A0QFB7
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pup--protein ligase | protein | 452 | 42% helix, 19% strand | A0QFB7 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.67 | 0.85 | 42 | empty |
| 2 | 67 | 0.52 | 0.86 | 16 | empty |
| 3 | 203 | 0.49 | 0.76 | 42 | empty |
| 4 | 172 | 0.48 | 0.77 | 26 | empty |
| 5 | 94 | 0.37 | 0.75 | 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 A0QFB7
- Elsewhere: UniProt A0QFB7 · AlphaFold DB A0QFB7
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