Solution structure of thermolysin digested microcin J25. Determined by solution NMR. Released 15 Jun 2004.
Explore 1S7P in 3D Show helices and sheets RCSB PDB PDBe
1S7P contains 0 α-helices and 3 β-strands across 2 chains. 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 | 2 | 1 | 1 |
| β-strand | 6-7 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19-20 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| microcin J25 | B | protein | 11 | Escherichia coli | Q9X2V7 (AlphaFold model) |
| microcin J25 | A | protein | 10 | Escherichia coli | Q9X2V7 (AlphaFold model) |
>1S7P_1 microcin J25 (chains B) VGIGTPISFYG
>1S7P_2 microcin J25 (chains A) GGAGHVPEYF
Structure of thermolysin cleaved microcin J25: extreme stability of a two-chain antimicrobial peptide devoid of covalent links. Rosengren, K.J., Blond, A., Afonso, C. et al. Biochemistry (2004) 43:4696-4702. DOI 10.1021/bi0361261 · 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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