› 2iha

Solution NMR

Amidated variant of CMrVIA conotoxin

Released:
DOI: 10.2210/pdb2iha/pdb
PDB entry 2iha coloured by chain, ensemble of 16 models, front view.
PDB entry 2iha coloured by chain, ensemble of 16 models, side view.
PDB entry 2iha coloured by chain, ensemble of 16 models, top view.
Source organism: synthetic construct
Primary publication:
Protein folding determinants: structural features determining alternative disulfide pairing in alpha- and chi/lambda-conotoxins.
Kang TS, Radić Z, Talley TT, Jois SD, Taylor P, Kini RM
Biochemistry 46 3338-55 (2007)
PMID: 17315952

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-162759 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lambda-conotoxin CMrVIA Chain: A
Molecule details ›
Chain: A
Length: 12 amino acids
Theoretical weight: 1.24 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand HYP 1 x HYP

Experiments and Validation Details

Entry percentile scores
Refinement method: Energy minimization, Molecular dynamics, Simulated annealing
Expression system: Not provided

Quick links

Citations

7 review citations

Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of Conus peptides.
Bulaj et al. (2008)
6 more

2 mentions without citation

Discovery, synthesis, and structure-activity relationships of conotoxins.
Akondi et al. (2014)
1 more