› 1k9b

X-ray diffraction
2.8Å resolution

Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation

Released:
DOI: 10.2210/pdb1k9b/pdb
PDB entry 1k9b coloured by chain, front view.
PDB entry 1k9b coloured by chain, side view.
PDB entry 1k9b coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation.
Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P
Eur J Biochem 242 122-31 (1996)
PMID: 8954162

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bowman-Birk type proteinase inhibitor Chain: A
Molecule details ›
Chain: A
Length: 58 amino acids
Theoretical weight: 6.43 KDa
Source organism: Glycine max
UniProt:
  • Canonical: P01055 (Residues: 45-102; Coverage: 64%)
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
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P4132
Unit cell:
a: 86.1Å b: 86.1Å c: 86.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.308

Quick links

Citations

10 review citations

The role of thiols and disulfides on protein stability.
Trivedi et al. (2009)
9 more

6 mentions without citation

Bowman-Birk Inhibitors: Insights into Family of Multifunctional Proteins and Peptides with Potential Therapeutical Applications.
Gitlin-Domagalska et al. (2020)
5 more