› 3w81

X-ray diffraction
2.3Å resolution

Human alpha-l-iduronidase

Released:
DOI: 10.2210/pdb3w81/pdb
PDB entry 3w81 coloured by chain, front view.
PDB entry 3w81 coloured by chain, side view.
PDB entry 3w81 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
Maita N, Tsukimura T, Taniguchi T, Saito S, Ohno K, Taniguchi H, Sakuraba H
Proc Natl Acad Sci U S A 110 14628-33 (2013)
PMID: 23959878

Function and Biology Details

Reaction catalysed: 
Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (5 distinct):
Alpha-L-iduronidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 627 amino acids
Theoretical weight: 70.12 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P35475 (Residues: 27-653; Coverage: 100%)
Gene name: IDUA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, FUC
Carbohydrate polymer
6 bound ligands:
Ligand NAG 3 x NAG
Ligand TLA 4 x TLA
Ligand GOL 2 x GOL
Ligand PO4 4 x PO4
Ligand CL 2 x CL
Ligand PO3 1 x PO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A, PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: R3
Unit cell:
a: 259.225Å b: 259.225Å c: 71.835Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.169 0.21
Expression system: Cricetulus griseus

Quick links

Citations

4 review citations

Dissecting conformational contributions to glycosidase catalysis and inhibition.
Speciale et al. (2014)
3 more

6 mentions without citation

Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
Maita et al. (2013)
5 more