Research workbench
AlphaFold monomer V2.0 prediction for trans-aconitate 2-methyltransferase (A7FGU8)
Analyse AlphaFold monomer V2.0 prediction for trans-aconitate 2-methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7FGU8
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Trans-aconitate 2-methyltransferase
- UniProt
- A7FGU8
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-aconitate 2-methyltransferase | protein | 258 | 41% helix, 24% strand | A7FGU8 |
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 | 356 | 0.74 | 0.85 | 51 | empty |
| 2 | 80 | 0.37 | 0.76 | 16 | empty |
| 3 | 66 | 0.34 | 0.76 | 17 | 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 A7FGU8
- Elsewhere: UniProt A7FGU8 · AlphaFold DB A7FGU8
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