Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (A0A391)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A391
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
- UniProt
- A0A391
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit H, chloroplastic | protein | 395 | 49% helix, 12% strand | A0A391 |
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 | 178 | 0.58 | 0.81 | 33 | empty |
| 2 | 57 | 0.49 | 0.86 | 16 | empty |
| 3 | 91 | 0.37 | 0.76 | 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 A0A391
- Elsewhere: UniProt A0A391 · AlphaFold DB A0A391
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