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AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (A6MM93)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6MM93
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
- UniProt
- A6MM93
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit H, chloroplastic | protein | 393 | 48% helix, 12% strand | A6MM93 |
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 | 64 | 0.52 | 0.86 | 21 | empty |
| 2 | 178 | 0.50 | 0.77 | 27 | empty |
| 3 | 82 | 0.36 | 0.76 | 15 | empty |
| 4 | 61 | 0.28 | 0.73 | 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 A6MM93
- Elsewhere: UniProt A6MM93 · AlphaFold DB A6MM93
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