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AlphaFold monomer V2.0 prediction for NAD(P)H-dependent FMN reductase ntnl (A0A455LN84)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-dependent FMN reductase ntnl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A455LN84
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1870f7A7de043458b061e1a3A5431D8b56e790fE
- Molecule
- NAD(P)H-dependent FMN reductase ntnl
- Pockets
- 1 · best druggability 0.38
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-dependent FMN reductase ntnl | protein | 201 | 43% helix, 21% strand | — |
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 | 53 | 0.38 | 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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