Research workbench
AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase dpche (H1VM35)
Analyse AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase dpche (H1VM35) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- H1VM35
- Type
- protein
- Length
- 470 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE5d7Dfb583170410b8F281b5c5D6ac753F1c4158
- UniProt
- H1VM35
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 470 | — | H1VM35 |
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 H1VM35
- Elsewhere: UniProt H1VM35 · AlphaFold DB H1VM35
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