› 4bp8

X-ray diffraction
2.4Å resolution

Oligopeptidase B from Trypanosoma brucei - open form

Released:
DOI: 10.2210/pdb4bp8/pdb
PDB entry 4bp8 coloured by chain, front view.
PDB entry 4bp8 coloured by chain, side view.
PDB entry 4bp8 coloured by chain, top view.
Source organism: Trypanosoma brucei
Primary publication:
Crystal structures of Trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes.
Canning P, Rea D, Morty RE, Fülöp V
PLoS One 8 e79349 (2013)
PMID: 24265767

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131237 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl endopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 715 amino acids
Theoretical weight: 81.63 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O76728 (Residues: 1-715; Coverage: 100%)
Gene name: opb
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 124.14Å b: 124.14Å c: 249.14Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.184 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Prolyl-specific peptidases for applications in food protein hydrolysis.
Mika et al. (2015)
9 other articles

6 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
5 more