› 2k46

Solution NMR

Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc)

Released:
DOI: 10.2210/pdb2k46/pdb
PDB entry 2k46 coloured by chain, ensemble of 20 models, front view.
PDB entry 2k46 coloured by chain, ensemble of 20 models, side view.
PDB entry 2k46 coloured by chain, ensemble of 20 models, top view.
Source organism: Xenopus laevis
Primary publication:
Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation.
Schallus T, Jaeckh C, Fehér K, Palma AS, Liu Y, Simpson JC, Mackeen M, Stier G, Gibson TJ, Feizi T, Pieler T, Muhle-Goll C
Mol Biol Cell 19 3404-14 (2008)
PMID: 18524852

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-563963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Malectin-A Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.2 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6INX3 (Residues: 27-213; Coverage: 75%)
Gene name: mlec-a
Sequence domains: Malectin domain
Structure domains: Galactose-binding lectin

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

56 review citations

Biological roles of glycans.
Varki A. (2017)
55 more

4 mentions without citation

Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation.
Schallus et al. (2008)
3 more