Research workbench
AlphaFold monomer V2.0 prediction for probable NADPH-dependent quinone reductase tdic (A7XRY6)
Analyse AlphaFold monomer V2.0 prediction for probable NADPH-dependent quinone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7XRY6
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Probable NADPH-dependent quinone reductase tdic
- UniProt
- A7XRY6
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable NADPH-dependent quinone reductase tdic | protein | 355 | 30% helix, 22% strand | A7XRY6 |
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 | 759 | 0.75 | 0.80 | 78 | empty |
| 2 | 104 | 0.39 | 0.76 | 23 | empty |
| 3 | 60 | 0.31 | 0.75 | 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 A7XRY6
- Elsewhere: UniProt A7XRY6 · AlphaFold DB A7XRY6
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