› 3isy

X-ray diffraction
2.61Å resolution

Crystal structure of an intracellular proteinase inhibitor (ipi, bsu11130) from bacillus subtilis at 2.61 A resolution

Released:
DOI: 10.2210/pdb3isy/pdb
PDB entry 3isy coloured by chain, front view.
PDB entry 3isy coloured by chain, side view.
PDB entry 3isy coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold.
Rigden DJ, Xu Q, Chang Y, Eberhardt RY, Finn RD, Rawlings ND
F1000Res 2 154 (2013)
PMID: 24555072

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153956 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Intracellular proteinase inhibitor Chain: A
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 14.29 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39804 (Residues: 1-119; Coverage: 100%)
Gene names: BSU11130, ipi
Sequence domains: Intracellular proteinase inhibitor
Structure domains: Intracellular proteinase inhibitor BsuPI

Ligands and Environments

1 bound ligand:
Ligand PG4 1 x PG4
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: I4122
Unit cell:
a: 73.586Å b: 73.586Å c: 132.923Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.243
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Mutational analysis of the pro-peptide of a marine intracellular subtilisin protease supports its role in inhibition.
Bjerga et al. (2018)

1 mention without citation

The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold.
Rigden et al. (2013)