Research workbench
AlphaFold monomer V2.0 prediction for bifunctional riboflavin KINASE/FMN adenylyltransferase (P47391)
Analyse AlphaFold monomer V2.0 prediction for bifunctional riboflavin KINASE/FMN… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P47391
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE4E71404165cB399da9a1A055946405dE4aC9870
- Molecule
- Bifunctional riboflavin KINASE/FMN adenylyltransferase
- UniProt
- P47391
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 30% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional riboflavin KINASE/FMN adenylyltransferase | protein | 269 | 30% helix, 33% strand | P47391 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.71 | 0.83 | 42 | empty |
| 2 | 168 | 0.58 | 0.82 | 22 | empty |
| 3 | 98 | 0.53 | 0.84 | 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 P47391
- Elsewhere: UniProt P47391 · AlphaFold DB P47391
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