Research workbench
AlphaFold monomer V2.0 prediction for FMN reductase (NADH) rutf (A9CHR3)
Analyse AlphaFold monomer V2.0 prediction for FMN reductase (NADH) rutf (A9CHR3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9CHR3
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa2a8313a9ac1C6C2Fd647eb71D26A934AC647886
- Molecule
- FMN reductase (NADH) rutf
- UniProt
- A9CHR3
- Pockets
- 1 · best druggability 0.49
Structure
1 distinct chain · 21% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN reductase (NADH) rutf | protein | 174 | 21% helix, 42% strand | A9CHR3 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.49 | 0.74 | 30 | 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 A9CHR3
- Elsewhere: UniProt A9CHR3 · AlphaFold DB A9CHR3
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