Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase chain 4 (A2BZX6)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase chain 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2BZX6
- Type
- protein
- Length
- 538 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- NAD(P)H-quinone oxidoreductase chain 4
- UniProt
- A2BZX6
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 72% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase chain 4 | protein | 538 | 72% helix, 4% strand | A2BZX6 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.59 | 0.90 | 18 | empty |
| 2 | 165 | 0.53 | 0.78 | 17 | empty |
| 3 | 191 | 0.51 | 0.77 | 36 | empty |
| 4 | 84 | 0.39 | 0.78 | 17 | 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 A2BZX6
- Elsewhere: UniProt A2BZX6 · AlphaFold DB A2BZX6
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