Research workbench
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MRA_3805 (A5U994)
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
- A5U994
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_3805
- UniProt
- A5U994
- Pockets
- 6 · best druggability 0.81
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_3805 | protein | 314 | 46% helix, 14% strand | A5U994 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.81 | 0.91 | 49 | empty |
| 2 | 280 | 0.79 | 0.91 | 46 | empty |
| 3 | 69 | 0.37 | 0.77 | 17 | empty |
| 4 | 73 | 0.31 | 0.74 | 13 | empty |
| 5 | 51 | 0.27 | 0.74 | 13 | 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 A5U994
- Elsewhere: UniProt A5U994 · AlphaFold DB A5U994
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