Research workbench
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MRA_0152 (A5TYM0)
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
- A5TYM0
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFB6bF9B65B1865F07ACb06897Cd13401125BdF0f
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0152
- UniProt
- A5TYM0
- Pockets
- 2 · best druggability 0.84
Structure
1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0152 | protein | 311 | 45% helix, 15% strand | A5TYM0 |
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 | 334 | 0.84 | 0.93 | 67 | empty |
| 2 | 110 | 0.44 | 0.78 | 22 | 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 A5TYM0
- Elsewhere: UniProt A5TYM0 · AlphaFold DB A5TYM0
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