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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (B5EZK7)
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
- B5EZK7
- Type
- protein
- Length
- 600 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7627501bA56CC95b4fadf15f9A6c07FbB6e86a05
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- B5EZK7
- Pockets
- 6 · best druggability 0.64
Structure
1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 600 | 41% helix, 17% strand | B5EZK7 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.64 | 0.79 | 41 | empty |
| 2 | 281 | 0.58 | 0.78 | 32 | empty |
| 3 | 52 | 0.49 | 0.86 | 14 | empty |
| 4 | 154 | 0.47 | 0.77 | 21 | empty |
| 5 | 90 | 0.33 | 0.74 | 12 | 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 B5EZK7
- Elsewhere: UniProt B5EZK7 · AlphaFold DB B5EZK7
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