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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (Q5X1B0)
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
- Q5X1B0
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2282b24c89f1D92FfBa894BD9f18ab55a2872194
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- Q5X1B0
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 417 | 52% helix, 12% strand | Q5X1B0 |
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 | 68 | 0.50 | 0.85 | 21 | empty |
| 2 | 80 | 0.46 | 0.81 | 16 | empty |
| 3 | 88 | 0.39 | 0.77 | 18 | empty |
| 4 | 86 | 0.35 | 0.75 | 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 Q5X1B0
- Elsewhere: UniProt Q5X1B0 · AlphaFold DB Q5X1B0
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