› 4q1u

X-ray diffraction
2.3Å resolution

Serum paraoxonase-1 by directed evolution with the K192Q mutation

Released:
DOI: 10.2210/pdb4q1u/pdb
PDB entry 4q1u coloured by chain, front view.
PDB entry 4q1u coloured by chain, side view.
PDB entry 4q1u coloured by chain, top view.
Source organism: hybrid
Primary publication:
Catalytic stimulation by restrained active-site floppiness--the case of high density lipoprotein-bound serum paraoxonase-1.
Ben-David M, Sussman JL, Maxwell CI, Szeler K, Kamerlin SCL, Tawfik DS
J Mol Biol 427 1359-1374 (2015)
PMID: 25644661

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165067 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serum paraoxonase/arylesterase 1 Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 39.57 KDa
Source organism: hybrid
Expression system: Escherichia coli BL21(DE3)
Structure domains: TolB, C-terminal domain

Ligands and Environments

5 bound ligands:
Ligand CA 2 x CA
Ligand LMT 1 x LMT
Ligand PO4 1 x PO4
Ligand CL 1 x CL
Ligand BR 1 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 93.514Å b: 93.514Å c: 144.007Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Perspective: Defining and quantifying the role of dynamics in enzyme catalysis.
Warshel et al. (2016)
8 more

3 mentions without citation

The Structure and Function of Paraoxonase-1 and Its Comparison to Paraoxonase-2 and -3.
Taler-Verčič et al. (2020)
2 more