Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (B8R4B1)
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
- B8R4B1
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf3C12C0D17117Fb2675C039f3b01b33237B9C2D1
- Molecule
- NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
- UniProt
- B8R4B1
- Pockets
- 3 · best druggability 0.57
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 | 393 | 49% helix, 12% strand | B8R4B1 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.57 | 0.78 | 36 | empty |
| 2 | 65 | 0.55 | 0.88 | 19 | empty |
| 3 | 65 | 0.33 | 0.76 | 11 | 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 B8R4B1
- Elsewhere: UniProt B8R4B1 · AlphaFold DB B8R4B1
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