X-ray diffraction
1.46Å resolution

Anionic trypsin variant S195A in complex with bovine pancreatic trypsin inhibitor (BPTI) determined to the 1.46 A resolution limit

Source organisms:
Primary publication:
Structure of a serine protease poised to resynthesize a peptide bond.
Proc. Natl. Acad. Sci. U.S.A. 106 11034-9 (2009)
PMID: 19549826

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Anionic trypsin-2 Chain: E
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.8 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
  • Canonical: P00763 (Residues: 24-246; Coverage: 97%)
Gene names: Prss2, Try2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chain: I
Molecule details ›
Chain: I
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P3221
Unit cell:
a: 91.933Å b: 91.933Å c: 61.135Å
α: 90° β: 90° γ: 120°
R R work R free
0.175 0.175 0.189
Expression system: Saccharomyces cerevisiae