› 1d6x

Solution NMR

THE STRUCTURE OF THE ANTIMICROBIAL PEPTIDE TRITRPTICIN BOUND TO MICELLES-A DISTINCT MEMBRANE-BOUND PEPTIDE FOLD

Released:
DOI: 10.2210/pdb1d6x/pdb
PDB entry 1d6x coloured by chain, ensemble of 19 models, front view.
PDB entry 1d6x coloured by chain, ensemble of 19 models, side view.
PDB entry 1d6x coloured by chain, ensemble of 19 models, top view.
Source organism: Synthetic construct
Primary publication:
Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold.
Schibli DJ, Hwang PM, Vogel HJ
Biochemistry 38 16749-55 (1999)
PMID: 10606506

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162154 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ANTIMICROBIAL PEPTIDE, TRITRPTICIN Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.91 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RESTRAINED SIMULATED ANNEALING MOLECULAR DYNAMICS
Expression system: Not provided

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Citations

14 review citations

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

5 mentions without citation

Antimicrobial and Antibiofilm Peptides.
Di Somma et al. (2020)
4 more