3rnz

X-ray diffraction
2.01Å resolution

Crystal structure of Bacillus Amyloliquefaciens Pyroglutamyl Peptidase I

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

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-155432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 223 amino acids
Theoretical weight: 24.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46107 (Residues: 1-215; Coverage: 100%)
Gene name: 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: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 289.89Å b: 45.36Å c: 68.09Å
α: 90° β: 91.34° γ: 90°
R-values:
R R work R free
0.176 0.174 0.209
Expression system: Escherichia coli