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AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (A4QL76)
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
- A4QL76
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
- UniProt
- A4QL76
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic | protein | 360 | 76% helix, 1% strand | A4QL76 |
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 | 395 | 0.70 | 0.81 | 57 | empty |
| 2 | 179 | 0.51 | 0.78 | 18 | empty |
| 3 | 100 | 0.48 | 0.80 | 19 | 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 A4QL76
- Elsewhere: UniProt A4QL76 · AlphaFold DB A4QL76
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