› 6can

X-ray diffraction
2.2Å resolution

Prolyl oligopeptidase mutant S477C from Pyrococcus furiosus

Released:
DOI: 10.2210/pdb6can/pdb
PDB entry 6can coloured by chain, front view.
PDB entry 6can coloured by chain, side view.
PDB entry 6can coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase.
Ellis-Guardiola K, Rui H, Beckner RL, Srivastava P, Sukumar N, Roux B, Lewis JC
Biochemistry 58 1616-1626 (2019)
PMID: 30786206

Function and Biology Details

Reaction catalysed: 
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175964 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
prolyl oligopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 616 amino acids
Theoretical weight: 70.94 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q51714 (Residues: 1-616; Coverage: 100%)
Sequence domains:
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 56.292Å b: 178.764Å c: 59.293Å
α: 90° β: 104.35° γ: 90°
R-values:
R R work R free
0.197 0.196 0.251
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.
Baharin et al. (2022)
7 other articles

2 mentions without citation

Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase.
Ellis-Guardiola et al. (2019)
1 more