PDBe 1a2z

X-ray diffraction
1.73Å resolution

PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 24.78 KDa
Source organism: Thermococcus litoralis
Expression system: Escherichia coli
UniProt:
  • Canonical: O07883 (Residues: 1-220; Coverage: 100%)
Gene names: OCC_03923, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 91.644Å b: 147.01Å c: 71.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.22
Expression system: Escherichia coli