› 2n6m

Solution NMR

Structural elucidation of the frog skin-derived peptide Esculentin-1a[Esc(1-21)NH2] inLipopolysaccharide and correlation with their function

Released:
DOI: 10.2210/pdb2n6m/pdb
PDB entry 2n6m coloured by chain, ensemble of 20 models, front view.
PDB entry 2n6m coloured by chain, ensemble of 20 models, side view.
PDB entry 2n6m coloured by chain, ensemble of 20 models, top view.
Source organism: Pelophylax lessonae
Primary publication:
NMR structure and binding of esculentin-1a (1-21)NH2 and its diastereomer to lipopolysaccharide: Correlation with biological functions.
Ghosh A, Bera S, Shai Y, Mangoni ML, Bhunia A
Biochim Biophys Acta 1858 800-12 (2016)
PMID: 26724203

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-154195 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Esculentin-1A Chain: A
Molecule details ›
Chain: A
Length: 21 amino acids
Theoretical weight: 2.19 KDa
Source organism: Pelophylax lessonae
Expression system: Not provided
UniProt:
  • Canonical: P40843 (Residues: 1-20; Coverage: 44%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 41%
Refinement method: torsion angle dynamics
Expression system: Not provided

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Citations

1 review citation

Bioinspired Designs, Molecular Premise and Tools for Evaluating the Ecological Importance of Antimicrobial Peptides.
Ongey et al. (2018)
7 other articles