› 4e3t

X-ray diffraction
1.65Å resolution

Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog

Released:
DOI: 10.2210/pdb4e3t/pdb
PDB entry 4e3t coloured by chain, front view.
PDB entry 4e3t coloured by chain, side view.
PDB entry 4e3t coloured by chain, top view.
Source organism: Brevundimonas diminuta
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: Brevundimonas diminuta
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

2 bound ligands:
Ligand ZN 6 x ZN
Ligand HLN 1 x HLN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 85.771Å b: 85.975Å c: 88.727Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.206
Expression system: Escherichia coli

Quick links

Citations

21 review citations

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

6 mentions without citation

Conformational dynamics and enzyme evolution.
Petrović et al. (2018)
5 more