1iu8

X-ray diffraction
1.6Å resolution

The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii

Released:

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: 206 amino acids
Theoretical weight: 22.67 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58321 (Residues: 1-206; Coverage: 100%)
Gene names: PH0596, 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: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: C2
Unit cell:
a: 104.899Å b: 66.479Å c: 76.396Å
α: 90° β: 128.68° γ: 90°
R-values:
R R work R free
0.189 0.189 0.214
Expression system: Escherichia coli