Research workbench
AlphaFold monomer V2.0 prediction for pup--protein ligase (C4LIK9)
Analyse AlphaFold monomer V2.0 prediction for pup--protein ligase (C4LIK9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C4LIK9
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- Pup--protein ligase
- UniProt
- C4LIK9
- Pockets
- 8 · best druggability 0.76
Structure
1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pup--protein ligase | protein | 477 | 42% helix, 17% strand | C4LIK9 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.76 | 0.97 | 20 | empty |
| 2 | 139 | 0.52 | 0.80 | 25 | empty |
| 3 | 210 | 0.50 | 0.76 | 27 | empty |
| 4 | 135 | 0.49 | 0.79 | 16 | empty |
| 5 | 133 | 0.44 | 0.77 | 25 | 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 C4LIK9
- Elsewhere: UniProt C4LIK9 · AlphaFold DB C4LIK9
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