› 1gqg

X-ray diffraction
1.7Å resolution

Quercetin 2,3-dioxygenase in complex with the inhibitor diethyldithiocarbamate

Released:
DOI: 10.2210/pdb1gqg/pdb
PDB entry 1gqg coloured by chain, front view.
PDB entry 1gqg coloured by chain, side view.
PDB entry 1gqg coloured by chain, top view.
Source organism: Aspergillus japonicus
Primary publication:
Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights.
Steiner RA, Kooter IM, Dijkstra BW
Biochemistry 41 7955-62 (2002)
PMID: 12069585

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Quercetin 2,3-dioxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 350 amino acids
Theoretical weight: 37.96 KDa
Source organism: Aspergillus japonicus
Expression system: Aspergillus awamori
UniProt:
  • Canonical: Q7SIC2 (Residues: 1-350; Coverage: 100%)
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand DCD 4 x DCD
Ligand CU 4 x CU
Ligand NAG 13 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 108.939Å b: 55.646Å c: 123.863Å
α: 90° β: 98.26° γ: 90°
R-values:
R R work R free
0.162 0.161 0.183
Expression system: Aspergillus awamori

Quick links

Citations

7 review citations

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
Clifton et al. (2006)
6 more

3 mentions without citation

Copper active sites in biology.
Solomon et al. (2014)
2 more