› 3sre

X-ray diffraction
1.99Å resolution

Serum paraoxonase-1 by directed evolution at pH 6.5

Released:
DOI: 10.2210/pdb3sre/pdb
PDB entry 3sre coloured by chain, front view.
PDB entry 3sre coloured by chain, side view.
PDB entry 3sre coloured by chain, top view.
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:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164037 (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

16 review citations

Quorum quenching: role in nature and applied developments.
Grandclément et al. (2016)
15 more

7 mentions without citation

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