› 1o7a

X-ray diffraction
2.25Å resolution

Human beta-Hexosaminidase B

Released:
DOI: 10.2210/pdb1o7a/pdb
PDB entry 1o7a coloured by chain, front view.
PDB entry 1o7a coloured by chain, side view.
PDB entry 1o7a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease.
Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W
J Mol Biol 328 669-81 (2003)
PMID: 12706724

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139695 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-hexosaminidase subunit beta Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 515 amino acids
Theoretical weight: 58.93 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07686 (Residues: 42-556; Coverage: 100%)
Gene names: HCC7, HEXB
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand GDL 6 x GDL
Ligand NAG 6 x NAG
Ligand EDO 15 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3121
Unit cell:
a: 163.931Å b: 163.931Å c: 244.717Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.236
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids.
Kolter et al. (2005)
6 more

9 mentions without citation

GM2 Gangliosidoses: Clinical Features, Pathophysiological Aspects, and Current Therapies.
Leal et al. (2020)
8 more