› 2hfr

Solution NMR

solution structure of antimicrobial peptide Fowlicidin 3

Released:
DOI: 10.2210/pdb2hfr/pdb
PDB entry 2hfr coloured by chain, ensemble of 20 models, front view.
PDB entry 2hfr coloured by chain, ensemble of 20 models, side view.
PDB entry 2hfr coloured by chain, ensemble of 20 models, top view.
Source organism: Gallus gallus
Primary publication:
Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities.
Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, Desilva U, Prakash O, Zhang G
FEBS J 274 418-28 (2007)
PMID: 17229147

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-173647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathelicidin-3 Chain: A
Molecule details ›
Chain: A
Length: 27 amino acids
Theoretical weight: 3.1 KDa
Source organism: Gallus gallus
Expression system: Not provided
UniProt:
  • Canonical: Q2IAL6 (Residues: 125-151; Coverage: 20%)
Gene name: CATHL3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: annealing
Expression system: Not provided

Quick links

Citations

7 review citations

Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action.
Mangoni et al. (2011)
6 more

1 mention without citation

The antimicrobial peptides and their potential clinical applications.
Lei et al. (2019)