› 2g9l

Solution NMR

The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction

Released:
DOI: 10.2210/pdb2g9l/pdb
PDB entry 2g9l coloured by chain, ensemble of 15 models, front view.
PDB entry 2g9l coloured by chain, ensemble of 15 models, side view.
PDB entry 2g9l coloured by chain, ensemble of 15 models, top view.
Source organism: Glandirana rugosa
Primary publication:
Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4.
Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH
Biochem Biophys Res Commun 352 592-7 (2007)
PMID: 17141187

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gaegurin-4 Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 3.76 KDa
Source organism: Glandirana rugosa
Expression system: Not provided
UniProt:
  • Canonical: P80398 (Residues: 44-80; Coverage: 64%)
Gene name: GGN4
Sequence domains: Frog antimicrobial peptide

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, molecular dynamics
Expression system: Not provided

Quick links

Citations

11 citation in other articles

High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion.
Perrin et al. (2014)
10 more

3 mentions without citation

Antimicrobial Peptides As Biologic and Immunotherapeutic Agents against Cancer: A Comprehensive Overview.
Roudi et al. (2017)
2 more