Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. Determined by solution NMR. Released 31 Oct 1993.
Explore 3CI2 in 3D Show helices and sheets RCSB PDB PDBe
3CI2 contains 1 α-helix and 6 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 | 23 | 1 | 1 |
| β-strand | 31 | 1 | 2 |
| α-helix | 32-42 | 11 | |
| β-strand | 50-52 | 3 | 3 |
| β-strand | 68-70 | 3 | 3 |
| β-strand | 75 | 1 | 2 |
| β-strand | 81 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chymotrypsin inhibitor 2 | A | protein | 66 | Hordeum vulgare | P01053 (AlphaFold model) |
>3CI2_1 CHYMOTRYPSIN INHIBITOR 2 (chains A) HNLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNIA QVPRVG
Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. Ludvigsen, S., Shen, H.Y., Kjaer, M. et al. J Mol Biol (1991) 222:621-635. DOI 10.1016/0022-2836(91)90500-6 · 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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