Research workbench
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MSMEG_0093 (A0QNM1)
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
- A0QNM1
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MSMEG_0093
- UniProt
- A0QNM1
- Pockets
- 2 · best druggability 0.88
Structure
1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MSMEG_0093 | protein | 317 | 45% helix, 13% strand | A0QNM1 |
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 | 807 | 0.88 | 0.91 | 77 | empty |
| 2 | 61 | 0.32 | 0.76 | 21 | 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 A0QNM1
- Elsewhere: UniProt A0QNM1 · AlphaFold DB A0QNM1
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