Research workbench
AlphaFold monomer V2.0 prediction for protein reduced wall acetylation 4 (Q9FXG3)
Analyse AlphaFold monomer V2.0 prediction for protein reduced wall acetylation 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FXG3
- Type
- protein
- Length
- 540 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8320c2083B5a06fc519aB744C68C78731D2131C3
- Molecule
- Protein reduced wall acetylation 4
- UniProt
- Q9FXG3
- Pockets
- 8 · best druggability 0.78
Structure
1 distinct chain · 73% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein reduced wall acetylation 4 | protein | 540 | 73% helix, 3% strand | Q9FXG3 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1084 | 0.78 | 0.79 | 73 | empty |
| 2 | 660 | 0.76 | 0.82 | 56 | empty |
| 3 | 274 | 0.64 | 0.81 | 34 | empty |
| 4 | 198 | 0.57 | 0.79 | 21 | empty |
| 5 | 187 | 0.55 | 0.79 | 18 | 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 Q9FXG3
- Elsewhere: UniProt Q9FXG3 · AlphaFold DB Q9FXG3
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