Research workbench
AlphaFold monomer V2.0 prediction for oxidoreductase pigb (Q5W270)
Analyse AlphaFold monomer V2.0 prediction for oxidoreductase pigb (Q5W270) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5W270
- Type
- protein
- Length
- 670 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE5FC0b4766EbeEdAA6231d28306a4B21e024C6F9
- Molecule
- Oxidoreductase pigb
- UniProt
- Q5W270
- Pockets
- 11 · best druggability 0.79
Structure
1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase pigb | protein | 670 | 46% helix, 18% strand | Q5W270 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.79 | 0.92 | 31 | empty |
| 2 | 583 | 0.77 | 0.83 | 61 | empty |
| 3 | 333 | 0.67 | 0.81 | 34 | empty |
| 4 | 246 | 0.66 | 0.82 | 27 | empty |
| 5 | 266 | 0.57 | 0.78 | 32 | 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 Q5W270
- Elsewhere: UniProt Q5W270 · AlphaFold DB Q5W270
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