Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (A0RMD0)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0RMD0
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- A0RMD0
- Pockets
- 2 · best druggability 0.41
Structure
1 distinct chain · 39% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 168 | 39% helix, 12% strand | A0RMD0 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.41 | 0.82 | 15 | empty |
| 2 | 68 | 0.31 | 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 A0RMD0
- Elsewhere: UniProt A0RMD0 · AlphaFold DB A0RMD0
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