1tpa

X-ray diffraction
1.9Å resolution

THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cationic trypsin Chain: E
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
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
Expression system: Not provided
UniProt:
  • 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 75.5Å b: 84.4Å c: 122.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Not provided