Research workbench
AlphaFold monomer V2.0 prediction for probable S-adenosylmethionine- dependent methyltransferase AT5G38100 (Q9LS10)
Analyse AlphaFold monomer V2.0 prediction for probable S-adenosylmethionine- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LS10
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Probable S-adenosylmethionine-dependent methyltransferase AT5G38100
- UniProt
- Q9LS10
- Pockets
- 3 · best druggability 0.84
Structure
1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable S-adenosylmethionine-dependent methyltransferase AT5G38100 | protein | 359 | 43% helix, 18% strand | Q9LS10 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.84 | 0.95 | 54 | empty |
| 2 | 72 | 0.41 | 0.80 | 12 | empty |
| 3 | 83 | 0.35 | 0.75 | 19 | 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 Q9LS10
- Elsewhere: UniProt Q9LS10 · AlphaFold DB Q9LS10
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