X-ray diffraction
2.68Å resolution

Crystal structure of a dioxygenase in the Crotonase superfamily in P21, A319C mutant

Source organism: Streptomyces toyocaensis
Primary publication:
Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.
Acta Crystallogr D Struct Biol 73 573-580 (2017)
PMID: 28695857

Function and Biology Details

Reaction catalysed:
(3,5-dihydroxyphenyl)acetyl-CoA + O(2) = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-185150 (preferred)
Entry contents:
1 distinct polypeptide molecule
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 438 amino acids
Theoretical weight: 48.27 KDa
Source organism: Streptomyces toyocaensis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q8KLK7 (Residues: 1-438; Coverage: 100%)
Gene name: BU52_01220
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 139.723Å b: 170.658Å c: 155.765Å
α: 90° β: 89.89° γ: 90°
R R work R free
0.197 0.193 0.215
Expression system: Escherichia coli BL21(DE3)