Research workbench
AlphaFold monomer V2.0 prediction for degv domain-containing protein LIN2658 (Q927X9)
Analyse AlphaFold monomer V2.0 prediction for degv domain-containing protein LIN2658… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q927X9
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC9F16D6B50D34396A80f1DDB90a4cb8b6C3C595c
- Molecule
- Degv domain-containing protein LIN2658
- UniProt
- Q927X9
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 43% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Degv domain-containing protein LIN2658 | protein | 283 | 43% helix, 25% strand | Q927X9 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.73 | 0.95 | 29 | empty |
| 2 | 65 | 0.41 | 0.80 | 17 | empty |
| 3 | 64 | 0.36 | 0.78 | 19 | empty |
| 4 | 53 | 0.34 | 0.78 | 15 | 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 Q927X9
- Elsewhere: UniProt Q927X9 · AlphaFold DB Q927X9
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