Research workbench
AlphaFold monomer V2.0 prediction for pup--protein ligase (A0PQT1)
Analyse AlphaFold monomer V2.0 prediction for pup--protein ligase (A0PQT1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0PQT1
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Pup--protein ligase
- UniProt
- A0PQT1
- Pockets
- 6 · best druggability 0.69
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 | A0PQT1 |
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 | 231 | 0.69 | 0.86 | 41 | empty |
| 2 | 62 | 0.53 | 0.87 | 17 | empty |
| 3 | 118 | 0.45 | 0.78 | 26 | empty |
| 4 | 122 | 0.44 | 0.77 | 23 | empty |
| 5 | 125 | 0.40 | 0.75 | 21 | 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 A0PQT1
- Elsewhere: UniProt A0PQT1 · AlphaFold DB A0PQT1
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