Research workbench
AlphaFold monomer V2.0 prediction for bifunctional F420 biosynthesis protein fbib (Q82DE3)
Analyse AlphaFold monomer V2.0 prediction for bifunctional F420 biosynthesis protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q82DE3
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3B8980aa24D16c478Ffda87D4df057cca6FC37da
- Molecule
- Bifunctional F420 biosynthesis protein fbib
- UniProt
- Q82DE3
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional F420 biosynthesis protein fbib | protein | 423 | 39% helix, 22% strand | Q82DE3 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.67 | 0.77 | 56 | empty |
| 2 | 151 | 0.54 | 0.81 | 23 | empty |
| 3 | 310 | 0.52 | 0.74 | 30 | empty |
| 4 | 136 | 0.51 | 0.80 | 19 | 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 Q82DE3
- Elsewhere: UniProt Q82DE3 · AlphaFold DB Q82DE3
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