3lac

X-ray diffraction
2Å resolution

Crystal structure of Bacillus anthracis pyrrolidone-carboxylate peptidase, pcP

Released:
Source organism: Bacillus anthracis
Entry authors: Anderson SM, Wawrzak Z, Onopriyenko O, Hasseman J, Edwards A, Savchenko A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 23.79 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q81NT5 (Residues: 1-215; Coverage: 100%)
Gene names: BAS2875, BA_3090, GBAA_3090, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

2 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P4322
Unit cell:
a: 78.55Å b: 78.55Å c: 141.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.223
Expression system: Escherichia coli