› 2lhw

Solution NMR

Tri-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat

Released:
DOI: 10.2210/pdb2lhw/pdb
PDB entry 2lhw coloured by chain, ensemble of 39 models, front view.
PDB entry 2lhw coloured by chain, ensemble of 39 models, side view.
PDB entry 2lhw coloured by chain, ensemble of 39 models, top view.
Source organism: synthetic construct
Primary publication:
Deciphering structural elements of mucin glycoprotein recognition.
Borgert A, Heimburg-Molinaro J, Song X, Lasanajak Y, Ju T, Liu M, Thompson P, Ragupathi G, Barany G, Smith DF, Cummings RD, Live D
ACS Chem Biol 7 1031-9 (2012)
PMID: 22444368

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162897 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MUC2 Mucin Domain Peptide Chain: A
Molecule details ›
Chain: A
Length: 9 amino acids
Theoretical weight: 782 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand A2G 3 x A2G
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: torsion space simulated annealing
Expression system: Not provided

Quick links

Citations

10 review citations

Protein glycosylation in cancer.
Stowell et al. (2015)
9 more

3 mentions without citation

The Biological Synthesis and the Function of Mucin 2 in Pseudomyxoma Peritonei.
Lin et al. (2021)
2 more