Dipeptide removal from MccJ25 yields a new lasso peptide delta-VG. Determined by solution NMR. Released 9 Sept 2026.
Explore 23FQ in 3D Show helices and sheets RCSB PDB PDBe
23FQ contains 1 α-helix and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 1 |
| α-helix | 8 | 1 | |
| β-strand | 17-18 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Microcin J25 | A | protein | 19 | Escherichia coli | Q9X2V7 (AlphaFold model) |
>23FQ_1 Microcin J25 (chains A) GGAGHVPEYFIGTPISFYG
Chemoenzymatic Modification of Microcin J25 with Single-Residue Precision Provides New-to-Nature Lasso Peptides. Tsai, C.Y., Chung, H.W., Huang, Y.P. et al. JACS Au (2026) 6:4618-4625. DOI 10.1021/jacsau.6c00700 · PubMed
Other PDB entries of the same protein (UniProt Q9X2V7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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