› 2zox

X-ray diffraction
1.9Å resolution

Crystal Structure of the Covalent Intermediate of Human Cytosolic beta-Glucosidase

Released:
DOI: 10.2210/pdb2zox/pdb
PDB entry 2zox coloured by chain, front view.
PDB entry 2zox coloured by chain, side view.
PDB entry 2zox coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase.
Noguchi J, Hayashi Y, Baba Y, Okino N, Kimura M, Ito M, Kakuta Y
Biochem Biophys Res Commun 374 549-52 (2008)
PMID: 18662675

Function and Biology Details

Reactions catalysed: 
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
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-190531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 469 amino acids
Theoretical weight: 53.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H227 (Residues: 1-469; Coverage: 100%)
Gene names: CBG, CBGL1, GBA3
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

7 bound ligands:
Ligand GLC 1 x GLC
Ligand PNG 1 x PNG
Ligand MG 2 x MG
Ligand PO4 1 x PO4
Ligand PLM 2 x PLM
Ligand OLA 1 x OLA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 66.12Å b: 82.529Å c: 91.673Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.226
Expression system: Escherichia coli

Quick links

Citations

4 review citations

β-Glucosidases.
Ketudat Cairns et al. (2010)
3 more

4 mentions without citation

Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.
Lee et al. (2018)
3 more