PDBe 1ab9

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Tyr-|-, Trp-|-, Phe-|-, Leu-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin A chain A Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chain: B
Molecule details ›
Chain: B
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Structure domains: Trypsin-like serine proteases
Chymotrypsin A chain C Chain: C
Molecule details ›
Chain: C
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Structure domains: Trypsin-like serine proteases
PENTAPEPTIDE (TPGVY) Chain: D
Molecule details ›
Chain: D
Length: 5 amino acids
Theoretical weight: 536 Da

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P42212
Unit cell:
a: 69.52Å b: 69.52Å c: 97.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.19