X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin Chain: T
Molecule details ›
Chain: T
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
  • Canonical: P00761 (Residues: 9-231; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Leech-derived tryptase inhibitor C Chain: L
Molecule details ›
Chain: L
Length: 46 amino acids
Theoretical weight: 4.75 KDa
Source organism: Hirudo medicinalis
Expression system: Saccharomyces cerevisiae
  • Canonical: P80424 (Residues: 1-46; Coverage: 100%)
Sequence domains: Kazal-type serine protease inhibitor domain
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 63.4Å b: 63.4Å c: 131.2Å
α: 90° β: 90° γ: 90°
R R work R free
0.197 0.197 not available
Expression system: Saccharomyces cerevisiae