2eo8

X-ray diffraction
2.3Å resolution

Crystal structure of a mutant pyrrolidone carboxyl peptidase (A199P) from P. furiosus

Released:
Source organism: Pyrococcus furiosus
Entry authors: Sakamoto K, Okazaki N, Yutani K

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-130730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 208 amino acids
Theoretical weight: 22.85 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: O73944 (Residues: 1-208; Coverage: 100%)
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: RIGAKU
Spacegroup: P21
Unit cell:
a: 47.636Å b: 104.423Å c: 104.267Å
α: 90° β: 95.27° γ: 90°
R-values:
R R work R free
0.187 0.185 0.235
Expression system: Escherichia coli