Research workbench
AlphaFold monomer V2.0 prediction for FMN reductase [NAD(P)H] (P94424)
Analyse AlphaFold monomer V2.0 prediction for FMN reductase [NAD(P)H] (P94424) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P94424
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3e8e3909a877B69b46206B47B350b98db3C5644b
- Molecule
- FMN reductase [NAD(P)H]
- UniProt
- P94424
- Pockets
- 2 · best druggability 0.44
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN reductase [NAD(P)H] | protein | 249 | 52% helix, 12% strand | P94424 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.44 | 0.73 | 27 | empty |
| 2 | 81 | 0.40 | 0.79 | 15 | empty |
Compared structures
- 1ZCH · Structure of the hypothetical oxidoreductase ycnd from bacillus subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1ZCH · Structure of the hypothetical oxidoreductase YcnD from Bacillus subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.99
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 P94424
- Elsewhere: UniProt P94424 · AlphaFold DB P94424
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