1EYB: Crystal Structure Of Apo Human Homogentisate Dioxygenase

Homogentisate dioxygenase (HGO) cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. HGO deficiency causes alkaptonuria (AKU), the first human disease shown to be inherited as a recessive Mendelian trait. Crystal structures of apo-HGO and HGO containing an iron ion have been determined at 1.9 and 2.3 A resolution, respectively. The HGO protomer, which contains a 280-residue N-terminal domain and a 140-residue C-terminal domain, associates as a hexamer arranged as a dimer of trimers. The active site iron ion is coordinated near the interface between subunits in the HGO trimer by a Glu and two His side chains. HGO represents a new structural class of dioxygenases. The largest group of AKU associated missense mutations affect residues located in regions of contact between subunits.
PDB ID: 1EYBDownload
MMDB ID: 14696
PDB Deposition Date: 2000/5/5
Updated in MMDB: 2000/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1EYB: hexameric; determined by author and by software (PISA,PQS)
Molecular Components in 1EYB
Label Count Molecule
Proteins (6 molecules)
Homogentisate 1,2-dioxygenase(Gene symbol: HGD)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB