Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (A1SE30)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1SE30
- Type
- protein
- Length
- 446 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- A1SE30
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 446 | 48% helix, 15% strand | A1SE30 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.52 | 0.76 | 40 | empty |
| 2 | 51 | 0.39 | 0.81 | 17 | empty |
| 3 | 67 | 0.37 | 0.78 | 15 | empty |
| 4 | 82 | 0.36 | 0.76 | 13 | 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 A1SE30
- Elsewhere: UniProt A1SE30 · AlphaFold DB A1SE30
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