Research workbench
AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase sdcf (C8VPE5)
Analyse AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase sdcf (C8VPE5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C8VPE5
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- FAD-dependent monooxygenase sdcf
- UniProt
- C8VPE5
- Pockets
- 2 · best druggability 0.83
Structure
1 distinct chain · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-dependent monooxygenase sdcf | protein | 479 | 40% helix, 24% strand | C8VPE5 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 623 | 0.83 | 0.87 | 89 | empty |
| 2 | 74 | 0.44 | 0.81 | 14 | 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 C8VPE5
- Elsewhere: UniProt C8VPE5 · AlphaFold DB C8VPE5
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