1ppe

X-ray diffraction
2Å resolution

THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
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
Trypsin inhibitor 1 Chain: I
Molecule details ›
Chain: I
Length: 29 amino acids
Theoretical weight: 3.28 KDa
Source organism: Cucurbita maxima
Expression system: Not provided
UniProt:
  • Canonical: P01074 (Residues: 1-29; Coverage: 100%)
Sequence domains: Squash family serine protease inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 59.28Å b: 55.47Å c: 74.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.151 not available
Expression system: Not provided