› 6gmu

X-ray diffraction
2.7Å resolution

Serum paraoxonase-1 by directed evolution with the L69G/H134R/F222S/T332S mutations

Released:
DOI: 10.2210/pdb6gmu/pdb
PDB entry 6gmu coloured by chain, front view.
PDB entry 6gmu coloured by chain, side view.
PDB entry 6gmu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Enzyme Evolution: An Epistatic Ratchet versus a Smooth Reversible Transition.
Ben-David M, Soskine M, Dubovetskyi A, Cherukuri KP, Dym O, Sussman JL, Liao Q, Szeler K, Kamerlin SCL, Tawfik DS
Mol Biol Evol 37 1133-1147 (2020)
PMID: 31873734

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-166779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serum Paraoxonase-1 by directed evolution with the L69G/H134R/F222S/T332S mutations Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 39.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: TolB, C-terminal domain

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand CL 3 x CL
Ligand B3P 1 x B3P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P43212
Unit cell:
a: 94.318Å b: 94.318Å c: 142.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.179 0.228
Expression system: Escherichia coli

Quick links

Citations

5 review citations

A mechanistic view of enzyme evolution.
Yang et al. (2020)
4 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)