Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (Q14FB0)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q14FB0
- Type
- protein
- Length
- 760 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB3eF4a844D48bDe7673985A59678e1f6278cb343
- Molecule
- NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic
- UniProt
- Q14FB0
- Pockets
- 8 · best druggability 0.68
Structure
1 distinct chain · 69% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic | protein | 760 | 69% helix, 3% strand | Q14FB0 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 501 | 0.68 | 0.79 | 37 | empty |
| 2 | 301 | 0.67 | 0.82 | 41 | empty |
| 3 | 228 | 0.64 | 0.82 | 29 | empty |
| 4 | 136 | 0.55 | 0.81 | 20 | empty |
| 5 | 153 | 0.43 | 0.74 | 17 | 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 Q14FB0
- Elsewhere: UniProt Q14FB0 · AlphaFold DB Q14FB0
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