› 2kr2

Solution NMR

Xenopus laevis malectin complexed with maltose (Glcalpha1-4Glc)

Released:
DOI: 10.2210/pdb2kr2/pdb
PDB entry 2kr2 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kr2 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kr2 coloured by chain, ensemble of 20 models, top view.
Source organism: Xenopus laevis
Primary publication:
Analysis of the specific interactions between the lectin domain of malectin and diglucosides.
Schallus T, Fehér K, Sternberg U, Rybin V, Muhle-Goll C
Glycobiology 20 1010-20 (2010)
PMID: 20466650

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-179765 (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
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: BGC, 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

Quick links

Citations

14 review citations

N-linked sugar-regulated protein folding and quality control in the ER.
Tannous et al. (2015)
13 more

2 mentions without citation

An LRR/Malectin Receptor-Like Kinase Mediates Resistance to Non-adapted and Adapted Powdery Mildew Fungi in Barley and Wheat.
Rajaraman et al. (2016)
1 more