X-ray diffraction
1.53Å resolution

Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements


Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Trypsin-1 Chain: A
Molecule details ›
Chain: A
Length: 242 amino acids
Theoretical weight: 26 KDa
Source organism: Salmo salar
  • Canonical: P35031 (Residues: 1-242; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P21212
Unit cell:
a: 71.43Å b: 83.26Å c: 30.87Å
α: 90° β: 90° γ: 90°
R R work R free
0.177 not available 0.229