Research workbench
AlphaFold monomer V2.0 prediction for E3 sumo-protein ligase NSE2 (Q32KY9)
Analyse AlphaFold monomer V2.0 prediction for E3 sumo-protein ligase NSE2 (Q32KY9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q32KY9
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x67Caacc81C91Ffe8C5b6E9623969278a00FCc789
- Molecule
- E3 sumo-protein ligase NSE2
- UniProt
- Q32KY9
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 54% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 sumo-protein ligase NSE2 | protein | 248 | 54% helix, 5% strand | Q32KY9 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.41 | 0.74 | 23 | empty |
| 2 | 103 | 0.40 | 0.76 | 17 | empty |
| 3 | 70 | 0.34 | 0.76 | 14 | empty |
| 4 | 54 | 0.29 | 0.76 | 11 | 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 Q32KY9
- Elsewhere: UniProt Q32KY9 · AlphaFold DB Q32KY9
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