› 1dum

Solution NMR

NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES

Released:
DOI: 10.2210/pdb1dum/pdb
PDB entry 1dum coloured by chain, ensemble of 10 models, front view.
PDB entry 1dum coloured by chain, ensemble of 10 models, side view.
PDB entry 1dum coloured by chain, ensemble of 10 models, top view.
Source organism: Xenopus laevis
Primary publication:
Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue.
Hara T, Kodama H, Kondo M, Wakamatsu K, Takeda A, Tachi T, Matsuzaki K
Biopolymers 58 437-46 (2001)
PMID: 11180056

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145626 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Magainin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 23 amino acids
Theoretical weight: 2.53 KDa
Source organism: Xenopus laevis
Expression system: Not provided
UniProt:
  • Canonical: P11006 (Residues: 267-289; Coverage: 8%)
Gene name: magainins

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

8 review citations

The relationship between peptide structure and antibacterial activity.
Powers et al. (2003)
7 more

4 mentions without citation

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