X-ray diffraction
1.9Å resolution

The crystal structure of the trypsin complex with synthetic heterochiral peptide

Source organism: Sus scrofa
Primary publication:
Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex.
J. Biomol. Struct. Dyn. 22 635-42 (2005)
PMID: 15842169

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: A
Molecule details ›
Chain: A
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
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 698 Da
Source organism: Sus scrofa
Expression system: Not provided

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 46.93Å b: 53.719Å c: 77.473Å
α: 90° β: 90° γ: 90°
R R work R free
0.155 0.153 0.178
Expression system: Not provided