› 2n0v

Solution NMR

Backbone 1H, Chemical Shift Assignments for Cn-APM1

Released:
DOI: 10.2210/pdb2n0v/pdb
PDB entry 2n0v coloured by chain, ensemble of 20 models, front view.
PDB entry 2n0v coloured by chain, ensemble of 20 models, side view.
PDB entry 2n0v coloured by chain, ensemble of 20 models, top view.
Source organism: Cocos nucifera
Primary publication:
Structural insights into Cn-AMP1, a short disulfide-free multifunctional peptide from green coconut water.
Santana MJ, de Oliveira AL, Queiroz Júnior LH, Mandal SM, Matos CO, Dias Rde O, Franco OL, Lião LM
FEBS Lett 589 639-44 (2015)
PMID: 25639464

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-163037 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antimicrobial peptide 1 Chain: A
Molecule details ›
Chain: A
Length: 10 amino acids
Theoretical weight: 875 Da
Source organism: Cocos nucifera
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 35%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

2 review citations

The role of antimicrobial peptides in plant immunity.
Campos et al. (2018)
1 more

3 mentions without citation

Antimicrobial Peptides from Fruits and Their Potential Use as Biotechnological Tools-A Review and Outlook.
Meneguetti et al. (2016)
2 more