› 2eqh

Solution NMR

Solution structure of growth-blocking peptide of the armyworm, Pseudaletia separata

Released:
DOI: 10.2210/pdb2eqh/pdb
PDB entry 2eqh coloured by chain, ensemble of 20 models, front view.
PDB entry 2eqh coloured by chain, ensemble of 20 models, side view.
PDB entry 2eqh coloured by chain, ensemble of 20 models, top view.
Source organism: Mythimna separata
Primary publication:
C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity.
Umetsu Y, Aizawa T, Muto K, Yamamoto H, Kamiya M, Kumaki Y, Mizuguchi M, Demura M, Hayakawa Y, Kawano K
J Biol Chem 284 29625-34 (2009)
PMID: 19710009

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173293 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Growth-blocking peptide, short form Chain: A
Molecule details ›
Chain: A
Length: 23 amino acids
Theoretical weight: 2.5 KDa
Source organism: Mythimna separata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27913 (Residues: 121-143; Coverage: 19%)
Sequence domains: Paralytic/GBP/PSP peptide

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Sea anemone peptide with uncommon β-hairpin structure inhibits acid-sensing ion channel 3 (ASIC3) and reveals analgesic activity.
Osmakov et al. (2013)
1 more

1 mention without citation

C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity.
Umetsu et al. (2009)