PDBe 2xe4

X-ray diffraction
1.65Å resolution

Structure of Oligopeptidase B from Leishmania major

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ANTIPAIN Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 607 Da
Source organism: Actinobacteria
Oligopeptidase b Chain: A
Molecule details ›
Chain: A
Length: 751 amino acids
Theoretical weight: 85.24 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4QHU7 (Residues: 1-731; Coverage: 100%)
Gene names: LMJF_09_0770, OPB
Sequence domains:
Structure domains:

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007, ESRF BEAMLINE BM14
Spacegroup: I222
Unit cell:
a: 95.478Å b: 142.776Å c: 208.919Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.14 0.178
Expression system: Escherichia coli BL21(DE3)