› 5t88

X-ray diffraction
1.9Å resolution

Prolyl oligopeptidase from Pyrococcus furiosus

Released:
DOI: 10.2210/pdb5t88/pdb
PDB entry 5t88 coloured by chain, front view.
PDB entry 5t88 coloured by chain, side view.
PDB entry 5t88 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: 70.92 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

3 bound ligands:
Ligand CL 4 x CL
Ligand TRS 11 x TRS
Ligand PRO 4 x PRO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 55.535Å b: 176.757Å c: 57.901Å
α: 90° β: 106.03° γ: 90°
R-values:
R R work R free
0.194 0.193 0.247
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Controlling the optical and catalytic properties of artificial metalloenzyme photocatalysts using chemogenetic engineering.
Zubi et al. (2022)
3 more

8 mentions without citation

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