› 2xwe

X-ray diffraction
2.31Å resolution

X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6S-(N'-(N-OCTYL)IMINO)-6-THIONOJIRIMYCIN IN THE ACTIVE SITE

Released:
DOI: 10.2210/pdb2xwe/pdb
PDB entry 2xwe coloured by chain, front view.
PDB entry 2xwe coloured by chain, side view.
PDB entry 2xwe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cyclodextrin-mediated crystallization of acid β-glucosidase in complex with amphiphilic bicyclic nojirimycin analogues.
Brumshtein B, Aguilar-Moncayo M, Benito JM, García Fernandez JM, Silman I, Shaaltiel Y, Aviezer D, Sussman JL, Futerman AH, Ortiz Mellet C
Org Biomol Chem 9 4160-7 (2011)
PMID: 21483943

Function and Biology Details

Reactions catalysed: 
D-glucosyl-N-acylsphingosine + H(2)O = D-glucose + N-acylsphingosine
D-galactosyl-N-acylsphingosine + H(2)O = D-galactose + N-acylsphingosine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137377 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lysosomal acid glucosylceramidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 505 amino acids
Theoretical weight: 56.59 KDa
Source organism: Homo sapiens
Expression system: Daucus carota
UniProt:
  • Canonical: P04062 (Residues: 40-536; Coverage: 100%)
Gene names: GBA, GBA1, GC, GLUC
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, FUC
Carbohydrate polymer
3 bound ligands:
Ligand PO4 2 x PO4
Ligand K 2 x K
Ligand AMF 2 x AMF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 68.142Å b: 96.693Å c: 82.97Å
α: 90° β: 102.84° γ: 90°
R-values:
R R work R free
0.153 0.15 0.213
Expression system: Daucus carota

Quick links

Citations

1 review citation

New Directions in Gaucher Disease.
Horowitz et al. (2016)
16 other articles

6 mentions without citation

β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.
Rohman et al. (2019)
5 more