› 7ywp

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oligopeptidase B Chain: A
Molecule details ›
Chain: A
Length: 676 amino acids
Theoretical weight: 78.26 KDa
Source organism: Serratia proteamaculans
Expression system: Escherichia coli
UniProt:
  • Canonical: B3VI58 (Residues: 2-677; Coverage: 100%)
Gene names: JKX24_00380, opdB
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand TCK 1 x TCK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 75.529Å b: 89.66Å c: 108.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.184 0.254
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Peptidases: Role and Function in Health and Disease.
Kos J. (2023)

1 mention without citation

Crystal Structure of Inhibitor-Bound Bacterial Oligopeptidase B in the Closed State: Similarity and Difference between Protozoan and Bacterial Enzymes.
Petrenko et al. (2023)