5fli

X-ray diffraction
2.15Å resolution

enzyme-substrate complex of Ni-quercetinase

Released:
Source organism: Streptomyces sp. FLA
Primary publication:
Quercetin 2,4-Dioxygenase Activates Dioxygen in a Side-On O2 -Ni Complex.
Angew. Chem. Int. Ed. Engl. 55 3281-4 (2016)
PMID: 26846734

Function and Biology Details

Reaction catalysed:
Quercetin + O(2) = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H(+)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cupin_2 domain-containing protein 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: 186 amino acids
Theoretical weight: 21.09 KDa
Source organism: Streptomyces sp. FLA
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A2VA43 (Residues: 1-186; Coverage: 100%)
Gene name: queD
Sequence domains: Cupin domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 101.396Å b: 113.752Å c: 105.003Å
α: 90° β: 96.45° γ: 90°
R-values:
R R work R free
0.197 0.195 0.232
Expression system: Escherichia coli BL21(DE3)