› 2e9l

X-ray diffraction
1.6Å resolution

Crystal Structure of human Cytosolic Neutral beta-Glycosylceramidase (Klotho-related Prote:KLrP) complex with Glucose and fatty acids

Released:
DOI: 10.2210/pdb2e9l/pdb
PDB entry 2e9l coloured by chain, front view.
PDB entry 2e9l coloured by chain, side view.
PDB entry 2e9l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase.
Hayashi Y, Okino N, Kakuta Y, Shikanai T, Tani M, Narimatsu H, Ito M
J Biol Chem 282 30889-900 (2007)
PMID: 17595169

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

4 bound ligands:
Ligand BGC 1 x BGC
Ligand PLM 2 x PLM
Ligand OLA 1 x OLA
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 66.035Å b: 83.976Å c: 94.882Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.221
Expression system: Escherichia coli

Quick links

Citations

20 review citations

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

6 mentions without citation

Improved transferase/hydrolase ratio through rational design of a family 1 β-glucosidase from Thermotoga neapolitana.
Lundemo et al. (2013)
5 more