Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase chain 4, chloroplastic (Q14FA8)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase chain 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q14FA8
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x58f53eCb168388AB0f1d3Cb9e5809dDe7f81eC02
- Molecule
- NAD(P)H-quinone oxidoreductase chain 4, chloroplastic
- UniProt
- Q14FA8
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 75% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase chain 4, chloroplastic | protein | 500 | 75% helix, 5% strand | Q14FA8 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.48 | 0.78 | 27 | empty |
| 2 | 161 | 0.47 | 0.75 | 19 | empty |
| 3 | 55 | 0.29 | 0.75 | 13 | 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 Q14FA8
- Elsewhere: UniProt Q14FA8 · AlphaFold DB Q14FA8
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