Research workbench
AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase phmc (Q0V6Q5)
Analyse AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase phmc (Q0V6Q5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0V6Q5
- Type
- protein
- Length
- 439 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaE274d0a9F86E84f92863832Ea0fD62d5b8B9348
- Molecule
- FAD-linked oxidoreductase phmc
- UniProt
- Q0V6Q5
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked oxidoreductase phmc | protein | 439 | 32% helix, 19% strand | Q0V6Q5 |
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 | 1148 | 0.79 | 0.80 | 93 | empty |
| 2 | 188 | 0.57 | 0.80 | 27 | empty |
| 3 | 53 | 0.32 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q0V6Q5
- Elsewhere: UniProt Q0V6Q5 · AlphaFold DB Q0V6Q5
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