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:
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
Pyrrolidone-carboxylate peptidase (preferred)
PDBe Complex ID:
PDB-CPX-129707 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 22.67 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like
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%)
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
X-ray source:
PHOTON FACTORY BEAMLINE BL-18B
Spacegroup:
C2
Expression system: Escherichia coli
