Research workbench
AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase nscc (E4V2N4)
Analyse AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase nscc (E4V2N4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E4V2N4
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x95359253bA527AB3762b6AD81b50414549F65387
- Molecule
- FAD-dependent monooxygenase nscc
- UniProt
- E4V2N4
- Pockets
- 2 · best druggability 0.79
Structure
1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-dependent monooxygenase nscc | protein | 412 | 37% helix, 23% strand | E4V2N4 |
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 | 1153 | 0.79 | 0.81 | 90 | empty |
| 2 | 60 | 0.34 | 0.77 | 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 E4V2N4
- Elsewhere: UniProt E4V2N4 · AlphaFold DB E4V2N4
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