Research workbench
AlphaFold monomer V2.0 prediction for trans-aconitate 2-methyltransferase (Q9I0S1)
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
- Q9I0S1
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Trans-aconitate 2-methyltransferase
- UniProt
- Q9I0S1
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-aconitate 2-methyltransferase | protein | 275 | 42% helix, 22% strand | Q9I0S1 |
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 | 376 | 0.75 | 0.85 | 57 | empty |
| 2 | 128 | 0.46 | 0.78 | 23 | empty |
| 3 | 91 | 0.39 | 0.77 | 24 | 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 Q9I0S1
- Elsewhere: UniProt Q9I0S1 · AlphaFold DB Q9I0S1
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