Research workbench
AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (Q6L1Y6)
Analyse AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (Q6L1Y6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6L1Y6
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e9272eA74C368dd3e84cE9A548B8C44a833C74C
- Molecule
- Ferredoxin--NADP reductase
- UniProt
- Q6L1Y6
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase | protein | 331 | 24% helix, 31% strand | Q6L1Y6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 698 | 0.72 | 0.79 | 80 | empty |
| 2 | 85 | 0.36 | 0.75 | 15 | empty |
| 3 | 52 | 0.27 | 0.74 | 14 | 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 Q6L1Y6
- Elsewhere: UniProt Q6L1Y6 · AlphaFold DB Q6L1Y6
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