CI-2, conformation 1. Determined by X-ray diffraction at 1.5 Å resolution. Released 25 Dec 2019.
Explore 6QIY in 3D Show helices and sheets RCSB PDB PDBe
6QIY contains 2 α-helices and 7 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 | 1 | 1 |
| α-helix | 8-10 | 3 | |
| β-strand | 14 | 1 | 2 |
| α-helix | 15-25 | 11 | |
| β-strand | 30-35 | 6 | 1 |
| β-strand | 48-53 | 6 | 1 |
| β-strand | 58 | 1 | 2 |
| β-strand | 59 | 1 | 1 |
| β-strand | 64-65 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Subtilisin-chymotrypsin inhibitor-2A | A | protein | 65 | Hordeum vulgare | P01053 (AlphaFold model) |
>6QIY_1 Subtilisin-chymotrypsin inhibitor-2A (chains A) DLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNIAE VPRVG
Engineering protein assemblies with allosteric control via monomer fold-switching. Campos, L.A., Sharma, R., Alvira, S. et al. Nat Commun (2019) 10:5703-5703. DOI 10.1038/s41467-019-13686-1 · PubMed
Other PDB entries of the same protein (UniProt P01053 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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