MolNFT v1 · #507683 · protein
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MRA_0153 (A5TYM1)
A5TYM1 · Putative S-adenosyl-L-methionine-dependent…: “AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MRA_0153…”. 3 pockets (best druggability 0.86). MolNFT v1 #507683 on GenesisL1: 3D…
- Accession
- A5TYM1
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0153
- UniProt
- A5TYM1
- Pockets
- 3 · best druggability 0.86
Structure
1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0153 | protein | 310 | 46% helix, 13% strand | A5TYM1 |
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 | 516 | 0.86 | 0.93 | 79 | empty |
| 2 | 97 | 0.43 | 0.79 | 24 | empty |
| 3 | 75 | 0.34 | 0.76 | 18 | 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 A5TYM1
- Elsewhere: UniProt A5TYM1 · AlphaFold DB A5TYM1
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