› 4bp9

X-ray diffraction
2.85Å resolution

Oligopeptidase B from Trypanosoma brucei with covalently bound antipain - closed form

Released:
DOI: 10.2210/pdb4bp9/pdb
PDB entry 4bp9 coloured by chain, front view.
PDB entry 4bp9 coloured by chain, side view.
PDB entry 4bp9 coloured by chain, top view.
Source organisms:
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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131238 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Prolyl endopeptidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 715 amino acids
Theoretical weight: 80.79 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:
ANTIPAIN Chains: G, H, I, J, K, L
Molecule details ›
Chains: G, H, I, J, K, L
Length: 4 amino acids
Theoretical weight: 608 Da
Source organism: Actinomycetes

Ligands and Environments

No bound ligands
1 modified residue:
Ligand FC0 6 x FC0

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 71.8Å b: 148.8Å c: 268Å
α: 90° β: 91° γ: 90°
R-values:
R R work R free
0.216 0.213 0.281
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

5 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)
4 more