Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit K, chloroplastic (A4GYR4)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit K… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4GYR4
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA282412EdfcE4C50dd88EF2f60821010627e7F46
- Molecule
- NAD(P)H-quinone oxidoreductase subunit K, chloroplastic
- UniProt
- A4GYR4
- Pockets
- 2 · best druggability 0.35
Structure
1 distinct chain · 34% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit K, chloroplastic | protein | 225 | 34% helix, 8% strand | A4GYR4 |
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 | 97 | 0.35 | 0.74 | 15 | empty |
| 2 | 57 | 0.28 | 0.74 | 12 | 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 A4GYR4
- Elsewhere: UniProt A4GYR4 · AlphaFold DB A4GYR4
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