X-ray diffraction
2.3Å resolution

Crystal Structure of Pf-PCP(1-204)-C


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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 213 amino acids
Theoretical weight: 23.39 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
  • Canonical: O73944 (Residues: 1-206; Coverage: 99%)
Gene names: PF1299, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 104.24Å b: 104.45Å c: 48.25Å
α: 90° β: 100.39° γ: 90°
R R work R free
0.197 0.197 0.234
Expression system: Escherichia coli