Crystal structure of bovine gamma-chymotrypsin. Determined by X-ray diffraction at 1.6 Å resolution. Released 20 Aug 1997.
Explore 1AB9 in 3D Show helices and sheets RCSB PDB PDBe
1AB9 contains 8 α-helices and 23 β-strands across 3 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 | 95 | 1 | 5 |
| β-strand | 100 | 1 | 5 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 6 |
| β-strand | 118 | 1 | 6 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| β-strand | 135-140 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 154 | 1 | 4 |
| α-helix | 155 | 1 | |
| 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 | 231-233 | 3 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 303 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gamma-chymotrypsin | A | protein | 13 | Bos taurus | P00766 (AlphaFold model) |
| Gamma-chymotrypsin | B | protein | 131 | Bos taurus | P00766 (AlphaFold model) |
| Gamma-chymotrypsin | C | protein | 97 | Bos taurus | P00766 (AlphaFold model) |
| Pentapeptide (TPGVY) | D | protein | 5 |
>1AB9_1 GAMMA-CHYMOTRYPSIN (chains A) CGVPAIQPVLSGL
>1AB9_2 GAMMA-CHYMOTRYPSIN (chains B) IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT CVTTGWGLTRY
>1AB9_3 GAMMA-CHYMOTRYPSIN (chains C) ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
>1AB9_4 PENTAPEPTIDE (TPGVY) (chains D) TPGVY
X-ray crystal structure of a dipeptide-chymotrypsin complex in an inhibitory interaction. Kashima, A., Inoue, Y., Sugio, S. et al. Eur J Biochem (1998) 255:12-23. DOI 10.1046/j.1432-1327.1998.2550012.x · PubMed
Other PDB entries of the same protein (UniProt P00766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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