5ndx

X-ray diffraction
2.2Å resolution

The bacterial orthologue of Human a-L-iduronidase does not need N-glycan post-translational modifications to be catalytically competent: Crystallography and QM/MM insights into Mucopolysaccharidosis I

Released:
Entry authors: Raich L, Valero-Gonzalez J, Castro-Lopez J, Millan C, Jimenez-Garcia MJ, Nieto P, Uson I, Hurtado-Guerrero R, Rovira C

Function and Biology Details

Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyosyl hydrolase Chain: A
Molecule details ›
Chain: A
Length: 621 amino acids
Theoretical weight: 68.88 KDa
Source organism: Rhizobium leguminosarum bv. trifolii
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1B8R7L2 (Residues: 1-621; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 39
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P6222
Unit cell:
a: 173.028Å b: 173.028Å c: 156.687Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.159 0.175
Expression system: Escherichia coli