Context dependence of protein secondary structure formation. The three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin carlsberg. Determined by solution NMR. Released 31 Oct 1993.
Explore 1CIS in 3D Show helices and sheets RCSB PDB PDBe
1CIS contains 1 α-helix and 8 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 | 47-51 | 5 | 1 |
| β-strand | 67-71 | 5 | 1 |
| β-strand | 72 | 1 | 3 |
| β-strand | 77 | 1 | 2 |
| β-strand | 78 | 1 | 3 |
| β-strand | 83 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hybrid protein formed from chymotrypsin inhibitor-2 | A | protein | 66 | Hordeum vulgare, Bacillus licheniformis | P01053 (AlphaFold model) |
>1CIS_1 HYBRID PROTEIN FORMED FROM CHYMOTRYPSIN INHIBITOR-2 (chains A) MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLEKQAVDNAYAEYRIDRVRLAVDKLDNIA QVPRVG
Context dependence of protein secondary structure formation: the three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin Carlsberg. Osmark, P., Sorensen, P., Poulsen, F.M. Biochemistry (1993) 32:11007-11014. DOI 10.1021/bi00092a009 · 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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