Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (B7MG50)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7MG50
- Type
- protein
- Length
- 600 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7beC3Ef9c210E66D52B594848B0A7dB52F1cD5c4
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- B7MG50
- Pockets
- 7 · best druggability 0.61
Structure
1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 600 | 43% helix, 17% strand | B7MG50 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.61 | 0.83 | 25 | empty |
| 2 | 155 | 0.50 | 0.78 | 20 | empty |
| 3 | 55 | 0.48 | 0.85 | 14 | empty |
| 4 | 129 | 0.46 | 0.78 | 25 | empty |
| 5 | 173 | 0.44 | 0.74 | 26 | 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 B7MG50
- Elsewhere: UniProt B7MG50 · AlphaFold DB B7MG50
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