PDBe 2g81

X-ray diffraction
1.55Å resolution

Crystal Structure of the Bowman-Birk Inhibitor from Vigna unguiculata Seeds in Complex with Beta-trypsin at 1.55 Angstrons Resolution


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
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
BOWMAN_BIRK domain-containing protein Chain: I
Molecule details ›
Chain: I
Length: 83 amino acids
Theoretical weight: 9.15 KDa
Source organism: Vigna unguiculata
  • Canonical: Q9S9H8 (Residues: 1-16, 17-78; Coverage: 99%)
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P212121
Unit cell:
a: 60.497Å b: 61.109Å c: 79.264Å
α: 90° β: 90° γ: 90°
R R work R free
0.155 0.154 0.169