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AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (A0ZZ90)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0ZZ90
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
- UniProt
- A0ZZ90
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic | protein | 363 | 75% helix, 1% strand | A0ZZ90 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.68 | 0.89 | 29 | empty |
| 2 | 188 | 0.53 | 0.77 | 25 | empty |
| 3 | 116 | 0.49 | 0.79 | 21 | empty |
| 4 | 200 | 0.46 | 0.74 | 20 | 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 A0ZZ90
- Elsewhere: UniProt A0ZZ90 · AlphaFold DB A0ZZ90
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