› 3sre

X-ray diffraction
1.99Å resolution

Serum paraoxonase-1 by directed evolution at pH 6.5

Released:
DOI: 10.2210/pdb3sre/pdb
PDB 3sre coloured by chain and viewed from the front.
PDB 3sre coloured by chain and viewed from the side.
PDB 3sre 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43212
Unit cell:
a: 93.653Å b: 93.653Å c: 143.705Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.22
Expression system: Escherichia coli

Quick links

Citations

14 review citations

A mechanistic view of enzyme evolution.
Yang et al. (2020)
13 more

3 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
2 more