7gch

X-ray diffraction
1.8Å resolution

STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero hexamer
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin A chain A Chain: E
Molecule details ›
Chain: E
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: F
Molecule details ›
Chain: F
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: G
Molecule details ›
Chain: G
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P42212
Unit cell:
a: 69.3Å b: 69.3Å c: 97.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 not available not available