› 2l2r

Solution NMR

Helical hairpin structure of a novel antimicrobial peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli)

Released:
DOI: 10.2210/pdb2l2r/pdb
PDB entry 2l2r coloured by chain, ensemble of 20 models, front view.
PDB entry 2l2r coloured by chain, ensemble of 20 models, side view.
PDB entry 2l2r coloured by chain, ensemble of 20 models, top view.
Source organism: Echinochloa crus-galli
Primary publication:
Disulfide-stabilized helical hairpin structure and activity of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).
Nolde SB, Vassilevski AA, Rogozhin EA, Barinov NA, Balashova TA, Samsonova OV, Baranov YV, Feofanov AV, Egorov TA, Arseniev AS, Grishin EV
J Biol Chem 286 25145-53 (2011)
PMID: 21561864

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162861 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antimicrobial peptide EcAMP1 Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.29 KDa
Source organism: Echinochloa crus-galli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 47%
Refinement method: simulated annealing

Quick links

Citations

18 review citations

Antimicrobial Peptides from Plants.
Tam et al. (2015)
17 more

11 mentions without citation

Plant Antimicrobial Peptides: State of the Art, In Silico Prediction and Perspectives in the Omics Era.
Dos Santos-Silva et al. (2020)
10 more