Research workbench
AlphaFold monomer V2.0 prediction for pup--protein ligase (Q828I4)
Analyse AlphaFold monomer V2.0 prediction for pup--protein ligase (Q828I4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q828I4
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Pup--protein ligase
- UniProt
- Q828I4
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pup--protein ligase | protein | 453 | 42% helix, 19% strand | Q828I4 |
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 | 90 | 0.76 | 0.98 | 20 | empty |
| 2 | 222 | 0.51 | 0.76 | 35 | empty |
| 3 | 148 | 0.48 | 0.78 | 26 | empty |
| 4 | 160 | 0.46 | 0.76 | 25 | empty |
| 5 | 65 | 0.39 | 0.79 | 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 Q828I4
- Elsewhere: UniProt Q828I4 · AlphaFold DB Q828I4
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