X-ray diffraction
1.5Å resolution

Crystal structure of Bacillus amyloliquefaciens pyroglutamyl peptidase I and terpyridine platinum(II)

Source organism: Bacillus amyloliquefaciens
Primary publication:
Terpyridine platinum(II) complexes inhibit cysteine proteases by binding to active-site cysteine.
J. Biomol. Struct. Dyn. 29 267-82 (2011)
PMID: 21875148

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
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
  • 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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: C2
Unit cell:
a: 290.32Å b: 45.52Å c: 67.99Å
α: 90° β: 91.48° γ: 90°
R R work R free
0.18 0.179 0.205
Expression system: Escherichia coli