› 4b1q

Solution NMR

NMR structure of the glycosylated conotoxin CcTx from Conus consors

Released:
DOI: 10.2210/pdb4b1q/pdb
PDB entry 4b1q coloured by chain, ensemble of 20 models, front view.
PDB entry 4b1q coloured by chain, ensemble of 20 models, side view.
PDB entry 4b1q coloured by chain, ensemble of 20 models, top view.
Source organism: Conus consors
Primary publication:
Structure of the O-glycosylated conopeptide CcTx from Conus consors venom.
Hocking HG, Gerwig GJ, Dutertre S, Violette A, Favreau P, Stöcklin R, Kamerling JP, Boelens R
Chemistry 19 870-9 (2013)
PMID: 23281027

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Conotoxin CcTx Chain: P
Molecule details ›
Chain: P
Length: 30 amino acids
Theoretical weight: 3.23 KDa
Source organism: Conus consors
UniProt:
  • Canonical: P58928 (Residues: 1-30; Coverage: 100%)

Ligands and Environments

Carbohydrate polymer : NEW Components: A2G, GAL, GXL, NDG
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand HYP 3 x HYP

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 72%
Refinement method: CYANA AND CNS

Quick links

Citations

7 review citations

Incorporation of post-translational modified amino acids as an approach to increase both chemical and biological diversity of conotoxins and conopeptides.
Espiritu et al. (2014)
6 more

2 mentions without citation

Glycosylation of conotoxins.
Gerwig et al. (2013)
1 more