Research workbench
AlphaFold monomer V2.0 prediction for electron transfer flavoprotein beta subunit lysine methyltransferase (Q80ZM3)
Analyse AlphaFold monomer V2.0 prediction for electron transfer flavoprotein beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q80ZM3
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Electron transfer flavoprotein beta subunit lysine methyltransferase
- UniProt
- Q80ZM3
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Electron transfer flavoprotein beta subunit lysine methyltransferase | protein | 255 | 39% helix, 17% strand | Q80ZM3 |
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 | 569 | 0.73 | 0.80 | 58 | empty |
| 2 | 80 | 0.56 | 0.87 | 22 | empty |
| 3 | 69 | 0.33 | 0.75 | 15 | 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 Q80ZM3
- Elsewhere: UniProt Q80ZM3 · AlphaFold DB Q80ZM3
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