Complex of two fragments of CI2 [(1-40)(DOT)(41-64)]. Determined by solution NMR. Released 29 Jan 1996.
Explore 1CIR in 3D Show helices and sheets RCSB PDB PDBe
1CIR contains 3 α-helices and 2 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 |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 13-15 | 3 | |
| α-helix | 16-20 | 5 | |
| β-strand | 30-32 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 48-50 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chymotrypsin inhibitor 2 | A | protein | 40 | Hordeum vulgare | P01053 (AlphaFold model) |
| Chymotrypsin inhibitor 2 | B | protein | 24 | Hordeum vulgare | P01053 (AlphaFold model) |
>1CIR_1 CHYMOTRYPSIN INHIBITOR 2 (chains A) MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTS
>1CIR_2 CHYMOTRYPSIN INHIBITOR 2 (chains B) EYRIDRVRLFVDKLDNIAQVPRVG
Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism. Neira, J.L., Davis, B., Ladurner, A.G. et al. Structure (1996) 1:189-208. DOI 10.1016/S1359-0278(96)00031-4 · 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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