Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (B5ZYL5)
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
- B5ZYL5
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- B5ZYL5
- Pockets
- 2 · best druggability 0.54
Structure
1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 396 | 52% helix, 13% strand | B5ZYL5 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.54 | 0.87 | 17 | empty |
| 2 | 119 | 0.51 | 0.81 | 29 | 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 B5ZYL5
- Elsewhere: UniProt B5ZYL5 · AlphaFold DB B5ZYL5
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