› 1v04

X-ray diffraction
2.2Å resolution

serum paraoxonase by directed evolution

Released:
DOI: 10.2210/pdb1v04/pdb
PDB entry 1v04 coloured by chain, front view.
PDB entry 1v04 coloured by chain, side view.
PDB entry 1v04 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes.
Harel M, Aharoni A, Gaidukov L, Brumshtein B, Khersonsky O, Meged R, Dvir H, Ravelli RB, McCarthy A, Toker L, Silman I, Sussman JL, Tawfik DS
Nat Struct Mol Biol 11 412-9 (2004)
PMID: 15098021

Function and Biology Details

Reactions catalysed: 
A phenyl acetate + H(2)O = a phenol + acetate
An N-acyl-L-homoserine lactone + H(2)O = an N-acyl-L-homoserine
An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150943 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serum paraoxonase/arylesterase 1 Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 39.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P27170 (Residues: 1-355; Coverage: 99%)
Gene names: PON, PON1
Sequence domains: Arylesterase
Structure domains: TolB, C-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 98.44Å b: 98.44Å c: 139.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.217
Expression system: Escherichia coli

Quick links

Citations

72 review citations

Modulation of paraoxonase (PON1) activity.
Costa et al. (2005)
71 more

41 mentions without citation

Divergence and convergence in enzyme evolution: parallel evolution of paraoxonases from quorum-quenching lactonases.
Elias et al. (2012)
40 more