Research workbench
AlphaFold monomer V2.0 prediction for trans-aconitate 2-methyltransferase (Q02N15)
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
- Q02N15
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5DD335da0E7B6349A9761Bec7652a919dC6599C6
- Molecule
- Trans-aconitate 2-methyltransferase
- UniProt
- Q02N15
- Pockets
- 3 · best druggability 0.72
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 | Q02N15 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.72 | 0.84 | 52 | empty |
| 2 | 161 | 0.51 | 0.79 | 22 | empty |
| 3 | 52 | 0.29 | 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 Q02N15
- Elsewhere: UniProt Q02N15 · AlphaFold DB Q02N15
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