Research workbench
AlphaFold monomer V2.0 prediction for electron transfer flavoprotein subunit beta (P52040)
Analyse AlphaFold monomer V2.0 prediction for electron transfer flavoprotein subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P52040
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA340bF1534bceeae44fe12C7C9F6CF023b79E47e
- Molecule
- Electron transfer flavoprotein subunit beta
- UniProt
- P52040
- Pockets
- 1 · best druggability 0.65
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Electron transfer flavoprotein subunit beta | protein | 259 | 34% helix, 25% strand | P52040 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.65 | 0.83 | 41 | 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 P52040
- Elsewhere: UniProt P52040 · AlphaFold DB P52040
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