Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (B2VIV4)
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
- B2VIV4
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe7fD32F422856e69Be28729279A8EB596328C29B
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- B2VIV4
- Pockets
- 4 · best druggability 0.54
Structure
1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 224 | 38% helix, 16% strand | B2VIV4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 267 | 0.54 | 0.76 | 33 | empty |
| 2 | 63 | 0.45 | 0.83 | 15 | empty |
| 3 | 77 | 0.39 | 0.78 | 19 | empty |
| 4 | 71 | 0.37 | 0.78 | 16 | 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 B2VIV4
- Elsewhere: UniProt B2VIV4 · AlphaFold DB B2VIV4
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