Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit M, chloroplastic (A2XVZ1)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit M… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2XVZ1
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
- UniProt
- A2XVZ1
- Pockets
- 2 · best druggability 0.36
Structure
1 distinct chain · 30% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit M, chloroplastic | protein | 220 | 30% helix, 9% strand | A2XVZ1 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.36 | 0.77 | 15 | empty |
| 2 | 58 | 0.29 | 0.74 | 15 | 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 A2XVZ1
- Elsewhere: UniProt A2XVZ1 · AlphaFold DB A2XVZ1
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