Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized phage-related protein LIN1244/LIN1753 (Q925X2)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized phage-related protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q925X2
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Uncharacterized phage-related protein LIN1244/LIN1753
- UniProt
- Q925X2
- Pockets
- 4 · best druggability 0.57
Structure
1 distinct chain · 50% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized phage-related protein LIN1244/LIN1753 | protein | 305 | 50% helix, 4% strand | Q925X2 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.57 | 0.75 | 43 | empty |
| 2 | 318 | 0.56 | 0.76 | 26 | empty |
| 3 | 84 | 0.31 | 0.73 | 13 | empty |
| 4 | 58 | 0.27 | 0.73 | 10 | 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 Q925X2
- Elsewhere: UniProt Q925X2 · AlphaFold DB Q925X2
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