› 4hho

X-ray diffraction
2.1Å resolution

Serum paraoxonase-1 by directed evolution with the H115W mutation

Released:
DOI: 10.2210/pdb4hho/pdb
PDB entry 4hho coloured by chain, front view.
PDB entry 4hho coloured by chain, side view.
PDB entry 4hho coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Catalytic metal ion rearrangements underline promiscuity and evolvability of a metalloenzyme.
Ben-David M, Wieczorek G, Elias M, Silman I, Sussman JL, Tawfik DS
J Mol Biol 425 1028-38 (2013)
PMID: 23318950

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-164543 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SERUM PARAOXONASE BY DIRECTED EVOLUTION Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 39.65 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: TolB, C-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P43212
Unit cell:
a: 93.782Å b: 93.782Å c: 145.158Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.212
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Progress in the development of enzyme-based nerve agent bioscavengers.
Nachon et al. (2013)
6 more

1 mention without citation

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