6gbl

X-ray diffraction
1.95Å resolution

Repertoires of functionally diverse enzymes through computational design at epistatic active-site positions

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parathion hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 36.63 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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 155.797Å b: 53.56Å c: 89.339Å
α: 90° β: 107.21° γ: 90°
R-values:
R R work R free
0.18 0.177 0.22
Expression system: Escherichia coli