Solution structure of the squash trypsin inhibitor EETI-II. Determined by solution NMR. Released 2 Oct 2007.
Explore 2IT7 in 3D Show helices and sheets RCSB PDB PDBe
2IT7 contains 2 α-helices and 4 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 | 8 | 1 | 1 |
| α-helix | 12-14 | 3 | |
| α-helix | 16 | 1 | |
| β-strand | 21 | 1 | 2 |
| β-strand | 26 | 1 | 1 |
| β-strand | 27 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trypsin inhibitor 2 | A | protein | 28 | P12071 (AlphaFold model) |
>2IT7_1 Trypsin inhibitor 2 (chains A) GCPRILMRCKQDSDCLAGCVCGPNGFCG
Knottin cyclization: Structure and stability of cyclic and linear squash inhibitors do not differ significantly. Heitz, A., Avrutina, O., Le-Nguyen, D. et al. To be published.
Other PDB entries of the same protein (UniProt P12071 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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