Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EY2

HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)

Summary for 1EY2
Entry DOI10.2210/pdb1ey2/pdb
Related1EYB
DescriptorHOMOGENTISATE 1,2-DIOXYGENASE, FE (II) ION (3 entities in total)
Functional Keywordsjelly roll, beta sandwich, oxidoreductase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight53704.43
Authors
Timm, D.E.,Titus, G.P.,Penalva, M.A.,Mueller, H.A.,de Cordoba, S.M. (deposition date: 2000-05-05, release date: 2000-11-05, Last modification date: 2021-11-03)
Primary citationTitus, G.P.,Mueller, H.A.,Burgner, J.,Rodriguez De Cordoba, S.,Penalva, M.A.,Timm, D.E.
Crystal structure of human homogentisate dioxygenase.
Nat.Struct.Biol., 7:542-546, 2000
Cited by
PubMed Abstract: 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.
PubMed: 10876237
DOI: 10.1038/76756
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon