› 4gy0

X-ray diffraction
1.85Å resolution

Round 18 Arylesterase Variant of Phosphotriesterase

Released:
DOI: 10.2210/pdb4gy0/pdb
PDB entry 4gy0 coloured by chain, front view.
PDB entry 4gy0 coloured by chain, side view.
PDB entry 4gy0 coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme.
Tokuriki N, Jackson CJ, Afriat-Jurnou L, Wyganowski KT, Tang R, Tawfik DS
Nat Commun 3 1257 (2012)
PMID: 23212386

Function and Biology Details

Reaction catalysed: 
An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141251 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parathion hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 36.21 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A434 (Residues: 34-365; Coverage: 99%)
Gene name: opd
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21212
Unit cell:
a: 86.109Å b: 86.366Å c: 89.192Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.241
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Evolutionary biochemistry: revealing the historical and physical causes of protein properties.
Harms et al. (2013)
23 more

1 mention without citation

In Silico Peptide Ligation: Iterative Residue Docking and Linking as a New Approach to Predict Protein-Peptide Interactions.
Diharce et al. (2019)