› 3srg

X-ray diffraction
2.19Å resolution

Serum paraoxonase-1 by directed evolution at pH 6.5 in complex with 2-hydroxyquinoline

Released:
DOI: 10.2210/pdb3srg/pdb
PDB 3srg coloured by chain and viewed from the front.
PDB 3srg coloured by chain and viewed from the side.
PDB 3srg coloured by chain and viewed from the top.
Source organism: synthetic construct
Primary publication:
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1.
Ben-David M, Elias M, Filippi JJ, Duñach E, Silman I, Sussman JL, Tawfik DS
J Mol Biol 418 181-96 (2012)
PMID: 22387469

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
serum paraoxonase Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 39.6 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: TolB, C-terminal domain

Ligands and Environments

5 bound ligands:
Ligand CA 3 x CA
Ligand OCH 1 x OCH
Ligand LMT 1 x LMT
Ligand BR 1 x BR
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 93.544Å b: 93.544Å c: 144.621Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.227
Expression system: Escherichia coli

Quick links

Citations

16 review citations

A PON for All Seasons: Comparing Paraoxonase Enzyme Substrates, Activity and Action including the Role of PON3 in Health and Disease.
Mohammed et al. (2022)
15 more

5 mentions without citation

Myeloperoxidase, paraoxonase-1, and HDL form a functional ternary complex.
Huang et al. (2013)
4 more