› 1pi2

X-ray diffraction
2.5Å resolution

REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS

Released:
DOI: 10.2210/pdb1pi2/pdb
PDB entry 1pi2 coloured by chain, front view.
PDB entry 1pi2 coloured by chain, side view.
PDB entry 1pi2 coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
Chen P, Rose J, Love R, Wei CH, Wang BC
J Biol Chem 267 1990-4 (1992)
PMID: 1730730

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133923 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bowman-Birk type proteinase inhibitor D-II Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 7.21 KDa
Source organism: Glycine max
Expression system: Not provided
UniProt:
  • Canonical: P01064 (Residues: 18-81; Coverage: 76%)
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P4132
Unit cell:
a: 89.96Å b: 89.96Å c: 89.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 not available not available
Expression system: Not provided

Quick links

Citations

7 review citations

Implications of antinutritional components in soybean foods.
Liener IE. (1994)
6 more

4 mentions without citation

Electrostatics in protein-protein docking.
Heifetz et al. (2002)
3 more