› 2wcg

X-ray diffraction
2.3Å resolution

X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site

Released:
DOI: 10.2210/pdb2wcg/pdb
PDB entry 2wcg coloured by chain, front view.
PDB entry 2wcg coloured by chain, side view.
PDB entry 2wcg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
6-Amino-6-deoxy-5,6-di-N-(N'-octyliminomethylidene)nojirimycin: synthesis, biological evaluation, and crystal structure in complex with acid beta-glucosidase.
Brumshtein B, Aguilar-Moncayo M, García-Moreno MI, Ortiz Mellet C, García Fernández JM, Silman I, Shaaltiel Y, Aviezer D, Sussman JL, Futerman AH
Chembiochem 10 1480-5 (2009)
PMID: 19437524

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
Carbohydrate polymer
4 bound ligands:
Ligand FUC 2 x FUC
Ligand SO4 12 x SO4
Ligand MT5 2 x MT5
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 68.311Å b: 96.827Å c: 83.234Å
α: 90° β: 104.34° γ: 90°
R-values:
R R work R free
0.138 0.135 0.194
Expression system: Daucus carota

Quick links

Citations

1 review citation

Animal Models for the Study of Gaucher Disease.
Cabasso et al. (2023)
25 other articles

4 mentions without citation

A Guided Tour of the Structural Biology of Gaucher Disease: Acid-β-Glucosidase and Saposin C.
Lieberman RL. (2011)
3 more