› 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:
DOI: 10.2210/pdb5ndx/pdb
PDB 5ndx coloured by chain and viewed from the front.
PDB 5ndx coloured by chain and viewed from the side.
PDB 5ndx coloured by chain and viewed from the top.
Source organism: Rhizobium leguminosarum bv. trifolii
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

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

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:
Ligand SO4 11 x SO4
Ligand 8U8 2 x 8U8
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

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