High resolution structure of bovine alpha-chymotrypsin. Determined by X-ray diffraction at 1.34 Å resolution. Released 14 Feb 2006.
Explore 1YPH in 3D Show helices and sheets RCSB PDB PDBe
1YPH contains 12 α-helices and 38 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 40-48 | 9 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 5 |
| β-strand | 118 | 1 | 5 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| β-strand | 135-140 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 6 |
| β-strand | 20-21 | 2 | 7 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 8 |
| β-strand | 40-48 | 9 | 8 |
| β-strand | 51-54 | 4 | 8 |
| α-helix | 56-58 | 3 | |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 72 | 1 | 9 |
| β-strand | 81-90 | 10 | 8 |
| β-strand | 104-108 | 5 | 8 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 7 |
| β-strand | 135-140 | 6 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 154 | 1 | 4 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 165-172 | 8 | |
| α-helix | 173-175 | 3 | |
| β-strand | 180-184 | 5 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 225-230 | 6 | 2 |
| α-helix | 231-243 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 154 | 1 | 9 |
| β-strand | 156-162 | 7 | 7 |
| α-helix | 165-172 | 8 | |
| α-helix | 173-175 | 3 | |
| β-strand | 180-184 | 5 | 7 |
| β-strand | 189 | 1 | 6 |
| β-strand | 198-203 | 6 | 7 |
| β-strand | 206-215 | 10 | 7 |
| β-strand | 225-230 | 6 | 7 |
| α-helix | 231-244 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CHYMOTRYPSIN A, chain A | A, B | protein | 13 | Bos taurus | P00766 (AlphaFold model) |
| CHYMOTRYPSIN A, chain B | C, D | protein | 131 | Bos taurus | P00766 (AlphaFold model) |
| CHYMOTRYPSIN A, chain C | E, F | protein | 97 | Bos taurus | P00766 (AlphaFold model) |
>1YPH_1 CHYMOTRYPSIN A, chain A (chains A, B) CGVPAIQPVLSGL
>1YPH_2 CHYMOTRYPSIN A, chain B (chains C, D) IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT CVTTGWGLTRY
>1YPH_3 CHYMOTRYPSIN A, chain C (chains E, F) ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
High resolution structure of native bovine alpha-chymotrypsin. Razeto, A., Galunsky, B., Kasche, V. et al. To be published.
Other PDB entries of the same protein (UniProt P00766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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