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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (B7MXG5)
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
- B7MXG5
- Type
- protein
- Length
- 600 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- B7MXG5
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 600 | 42% helix, 17% strand | B7MXG5 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 526 | 0.66 | 0.78 | 40 | empty |
| 2 | 323 | 0.64 | 0.80 | 50 | empty |
| 3 | 154 | 0.50 | 0.78 | 18 | empty |
| 4 | 64 | 0.47 | 0.84 | 17 | empty |
| 5 | 84 | 0.32 | 0.74 | 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 B7MXG5
- Elsewhere: UniProt B7MXG5 · AlphaFold DB B7MXG5
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