X-ray diffraction
2.3Å resolution

Trypsin inhibitor in complex with bovine trypsin variant X(SSWI)bT.B4

Source organism: Bos taurus
Primary publication:
Understanding protein-ligand interactions: the price of protein flexibility.
J. Mol. Biol. 335 1325-41 (2004)
PMID: 14729347

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Cationic trypsin Chain: T
Molecule details ›
Chain: T
Length: 223 amino acids
Theoretical weight: 23.35 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
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: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 55.05Å b: 57.97Å c: 68.53Å
α: 90° β: 90° γ: 90°
R R work R free
0.186 0.186 0.233
Expression system: Escherichia coli