3ivl

X-ray diffraction
2.2Å resolution

The Crystal Structure of the Inactive Peptidase Domain of a Putative Zinc Protease from Bordetella parapertussis to 2.2A

Released:
Source organism: Bordetella parapertussis
Entry authors: Stein AJ, Wu R, Keigher L, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-182104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Zinc protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 22.93 KDa
Source organism: Bordetella parapertussis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7W521 (Residues: 258-465; Coverage: 23%)
Gene name: BPP3483
Sequence domains: Peptidase M16 inactive domain
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R3
Unit cell:
a: 108.173Å b: 108.173Å c: 113.995Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.216 0.258
Expression system: Escherichia coli BL21(DE3)