2ebj

X-ray diffraction
1.9Å resolution

Crystal structure of pyrrolidone carboxyl peptidase from Thermus thermophilus

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Kumarevel TS, Karthe P, Agari Y, Kuramitsu S, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 192 amino acids
Theoretical weight: 21.15 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJW4 (Residues: 1-192; Coverage: 100%)
Gene name: TTHA0888
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: SPRING-8 BEAMLINE BL26B2
Spacegroup: C2221
Unit cell:
a: 51.913Å b: 118.382Å c: 143.581Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.257
Expression system: Escherichia coli BL21(DE3)