X-ray diffraction
1.25Å resolution

1.25 Angstrom Crystal Structure of Pyrrolidone-Carboxylate Peptidase (pcp) from Staphylococcus aureus

Entry authors: Minasov G, Wawrzak Z, Skarina T, Onopriyenko O, Peterson SN, 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

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Pyrrolidone-carboxylate peptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 23.6 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli
  • Canonical: Q5HCK7 (Residues: 1-212; Coverage: 100%)
Gene names: SACOL2714, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 42.79Å b: 81Å c: 119.91Å
α: 90° β: 90° γ: 90°
R R work R free
0.118 0.116 0.148
Expression system: Escherichia coli