Research workbench
AlphaFold monomer V2.0 prediction for bifunctional riboflavin KINASE/FMN adenylyltransferase (P22990)
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
- P22990
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Bifunctional riboflavin KINASE/FMN adenylyltransferase
- UniProt
- P22990
- Pockets
- 7 · best druggability 0.72
Structure
1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional riboflavin KINASE/FMN adenylyltransferase | protein | 311 | 33% helix, 28% strand | P22990 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 471 | 0.72 | 0.82 | 43 | empty |
| 2 | 298 | 0.65 | 0.81 | 30 | empty |
| 3 | 111 | 0.49 | 0.80 | 22 | empty |
| 4 | 90 | 0.46 | 0.81 | 18 | empty |
| 5 | 87 | 0.38 | 0.77 | 18 | 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 P22990
- Elsewhere: UniProt P22990 · AlphaFold DB P22990
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