X-ray diffraction
1.7Å 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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Trypsin-1 Chain: M
Molecule details ›
Chain: M
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P212121
Unit cell:
a: 44.944Å b: 48.269Å c: 83.102Å
α: 90° β: 90° γ: 90°
R R work R free
0.176 0.176 0.216