Research workbench
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase SACE_1742 (A4FAI5)
Analyse AlphaFold monomer V2.0 prediction for putative S-adenosyl-L… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4FAI5
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd614Ed90680C17d8553917A1D6e83dc1BC53A527
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase SACE_1742
- UniProt
- A4FAI5
- Pockets
- 2 · best druggability 0.88
Structure
1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase SACE_1742 | protein | 287 | 46% helix, 15% strand | A4FAI5 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.88 | 0.94 | 60 | empty |
| 2 | 98 | 0.47 | 0.81 | 20 | 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 A4FAI5
- Elsewhere: UniProt A4FAI5 · AlphaFold DB A4FAI5
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