1tab

X-ray diffraction
2.3Å resolution

STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only tetramer (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
Bowman-Birk type proteinase inhibitor Chain: I
Molecule details ›
Chain: I
Length: 82 amino acids
Theoretical weight: 9.14 KDa
Source organism: Vigna angularis
Expression system: Not provided
UniProt:
  • Canonical: P01058 (Residues: 1-82; Coverage: 100%)
Sequence domains: Bowman-Birk serine protease inhibitor family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 55.42Å b: 55.42Å c: 181.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 not available not available
Expression system: Not provided