PDBe 1gg6

X-ray diffraction
1.4Å resolution

CRYSTAL STRUCTURE OF GAMMA CHYMOTRYPSIN WITH N-ACETYL-PHENYLALANINE TRIFLUOROMETHYL KETONE BOUND AT THE ACTIVE SITE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin A chain A Chain: A
Molecule details ›
Chain: A
Length: 10 amino acids
Theoretical weight: 996 Da
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-10; Coverage: 4%)
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

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P42212
Unit cell:
a: 69.19Å b: 69.19Å c: 95.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.212