› 2l5r

Solution NMR

Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C

Released:
DOI: 10.2210/pdb2l5r/pdb
PDB entry 2l5r coloured by chain, ensemble of 20 models, front view.
PDB entry 2l5r coloured by chain, ensemble of 20 models, side view.
PDB entry 2l5r coloured by chain, ensemble of 20 models, top view.
Source organism: Alytes obstetricans
Primary publication:
Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c.
Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM
Biochim Biophys Acta 1808 1975-84 (2011)
PMID: 21565166

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124702 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alyteserin-1c Chain: A
Molecule details ›
Chain: A
Length: 23 amino acids
Theoretical weight: 2.27 KDa
Source organism: Alytes obstetricans
Expression system: Not provided
UniProt:
  • Canonical: H0USY4 (Residues: 1-23; Coverage: 100%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

4 review citations

ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.
Ahmad et al. (2013)
3 more

4 mentions without citation

Evaluation of the Antimicrobial Activity of Cationic Peptides Loaded in Surface-Modified Nanoliposomes against Foodborne Bacteria.
Cantor et al. (2019)
3 more