Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (A1ADD5)
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
- A1ADD5
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- A1ADD5
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 220 | 37% helix, 18% strand | A1ADD5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.58 | 0.76 | 37 | empty |
| 2 | 206 | 0.56 | 0.79 | 26 | empty |
| 3 | 105 | 0.48 | 0.80 | 23 | 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 A1ADD5
- Elsewhere: UniProt A1ADD5 · AlphaFold DB A1ADD5
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