The effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Determined by X-ray diffraction at 2.2 Å resolution. Released 31 Jan 1994.
Explore 1COA in 3D Show helices and sheets RCSB PDB PDBe
1COA contains 3 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 | 23 | 1 | 1 |
| α-helix | 25-27 | 3 | |
| β-strand | 31 | 1 | 2 |
| α-helix | 32-42 | 11 | |
| β-strand | 47-52 | 6 | 1 |
| α-helix | 55-58 | 4 | |
| β-strand | 65-70 | 6 | 1 |
| β-strand | 75 | 1 | 2 |
| β-strand | 76 | 1 | 1 |
| β-strand | 81-82 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chymotrypsin inhibitor 2 | I | protein | 64 | Hordeum vulgare | P01053 (AlphaFold model) |
>1COA_1 CHYMOTRYPSIN INHIBITOR 2 (chains I) MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNVAEV PRVG
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Jackson, S.E., Moracci, M., elMasry, N. et al. Biochemistry (1993) 32:11259-11269. DOI 10.1021/bi00093a001 · 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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