Research workbench
AlphaFold monomer V2.0 prediction for FAD:PROTEIN FMN transferase (P41780)
Analyse AlphaFold monomer V2.0 prediction for FAD:PROTEIN FMN transferase (P41780) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P41780
- Type
- protein
- Length
- 350 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- UniProt
- P41780
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 350 | — | P41780 |
Compared structures
- 3PND · FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins · an experimental structure of the same protein · chain A against C, TM-score 0.86
- 3PND · FAD binding by apbe protein from salmonella enterica: a new class of FAD binding proteins · an experimental structure of the same protein · chain A against C, TM-score 0.86
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 P41780
- Elsewhere: UniProt P41780 · AlphaFold DB P41780
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