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AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase peno (A0A0E3D8N6)
Analyse AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase peno… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A0E3D8N6
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x280f90Bba42f50710657E36c6D55B46307cf78ED
- Molecule
- FAD-linked oxidoreductase peno
- Pockets
- 4 · best druggability 0.87
Structure
1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked oxidoreductase peno | protein | 450 | 32% helix, 26% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 715 | 0.87 | 0.90 | 77 | empty |
| 2 | 257 | 0.54 | 0.76 | 39 | empty |
| 3 | 132 | 0.50 | 0.80 | 26 | empty |
| 4 | 60 | 0.40 | 0.81 | 17 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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