1BHG: Human Beta-Glucuronidase At 2.6 A Resolution

The X-ray structure of the homotetrameric lysosomal acid hydrolase, human beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution. The tetramer has approximate dihedral symmetry and each promoter consists of three structural domains with topologies similar to a jelly roll barrel, an immunoglobulin constant domain and a TIM barrel respectively. Residues 179-204 form a beta-hairpin motif similar to the putative lysosomal targeting motif of cathepsin D, supporting the view that lysosomal targeting has a structural basis. The active site of the enzyme is formed from a large cleft at the interface of two monomers. Residues Glu 451 and Glu 540 are proposed to be important for catalysis. The structure establishes a framework for understanding mutations that lead to the human genetic disease mucopolysaccharidosis VII, and for using the enzyme in anti-cancer therapy.
PDB ID: 1BHGDownload
MMDB ID: 6432
PDB Deposition Date: 1996/3/4
Updated in MMDB: 1998/11
Experimental Method:
x-ray diffraction
Resolution: 2.53  Å
Source Organism:
Similar Structures:
Biological Unit for 1BHG: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1BHG
Label Count Molecule
Proteins (4 molecules)
Beta-glucuronidase(Gene symbol: GUSB)
Molecule annotation
Chemicals (28 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB