› 3fp7

X-ray diffraction
1.46Å resolution

Anionic trypsin variant S195A in complex with bovine pancreatic trypsin inhibitor (BPTI) cleaved at the scissile bond (LYS15-ALA16) determined to the 1.46 A resolution limit

Released:
DOI: 10.2210/pdb3fp7/pdb
PDB entry 3fp7 coloured by chain, front view.
PDB entry 3fp7 coloured by chain, side view.
PDB entry 3fp7 coloured by chain, top view.
Source organisms:
Primary publication:
Structure of a serine protease poised to resynthesize a peptide bond.
Zakharova E, Horvath MP, Goldenberg DP
Proc Natl Acad Sci U S A 106 11034-9 (2009)
PMID: 19549826

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133398 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 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
UniProt:
  • 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: 15 amino acids
Theoretical weight: 1.72 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00974 (Residues: 36-50; Coverage: 19%)
Pancreatic trypsin inhibitor Chain: J
Molecule details ›
Chain: J
Length: 43 amino acids
Theoretical weight: 4.82 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00974 (Residues: 51-93; Coverage: 54%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

4 bound ligands:
Ligand EDO 5 x EDO
Ligand PG4 1 x PG4
Ligand CA 1 x CA
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P3221
Unit cell:
a: 91.969Å b: 91.969Å c: 61.001Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.175 0.186
Expression systems:
  • Saccharomyces cerevisiae
  • Not provided

Quick links

Citations

5 review citations

Mechanisms of macromolecular protease inhibitors.
Farady et al. (2010)
4 more

4 mentions without citation

Structure of a serine protease poised to resynthesize a peptide bond.
Zakharova et al. (2009)
3 more