MolNFT v1 · #260695 · protein
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H (A3PAP0)
A3PAP0: “AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H (A3PAP0)”. 3 pockets (best druggability 0.53). MolNFT v1 #260695 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A3PAP0
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- NAD(P)H-quinone oxidoreductase subunit H
- UniProt
- A3PAP0
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit H | protein | 395 | 51% helix, 12% strand | A3PAP0 |
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 | 163 | 0.53 | 0.80 | 23 | empty |
| 2 | 66 | 0.53 | 0.87 | 19 | empty |
| 3 | 58 | 0.30 | 0.75 | 10 | 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 A3PAP0
- Elsewhere: UniProt A3PAP0 · AlphaFold DB A3PAP0
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