Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (Q5NIN2)
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
- Q5NIN2
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- Q5NIN2
- Pockets
- 4 · best druggability 0.48
Structure
1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 417 | 51% helix, 12% strand | Q5NIN2 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.48 | 0.84 | 21 | empty |
| 2 | 111 | 0.43 | 0.77 | 14 | empty |
| 3 | 92 | 0.40 | 0.77 | 18 | empty |
| 4 | 99 | 0.35 | 0.73 | 16 | 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 Q5NIN2
- Elsewhere: UniProt Q5NIN2 · AlphaFold DB Q5NIN2
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