Research workbench
AlphaFold monomer V2.0 prediction for ferredoxin--NAD(P)(+) reductase fdr (D5IGG6)
Analyse AlphaFold monomer V2.0 prediction for ferredoxin--NAD(P)(+) reductase fdr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D5IGG6
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7EBA66f42a134ed5D9894Eb790da5698bF825Df0
- Molecule
- Ferredoxin--NAD(P)(+) reductase fdr
- UniProt
- D5IGG6
- Pockets
- 2 · best druggability 0.81
Structure
1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NAD(P)(+) reductase fdr | protein | 414 | 27% helix, 31% strand | D5IGG6 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 992 | 0.81 | 0.82 | 94 | empty |
| 2 | 74 | 0.35 | 0.76 | 12 | 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 D5IGG6
- Elsewhere: UniProt D5IGG6 · AlphaFold DB D5IGG6
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