› 2mn5

Solution NMR

NMR structure of Copsin

Released:
DOI: 10.2210/pdb2mn5/pdb
PDB entry 2mn5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2mn5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2mn5 coloured by chain, ensemble of 20 models, top view.
Source organism: Coprinopsis cinerea
Primary publication:
Copsin, a novel peptide-based fungal antibiotic interfering with the peptidoglycan synthesis.
Essig A, Hofmann D, Münch D, Gayathri S, Künzler M, Kallio PT, Sahl HG, Wider G, Schneider T, Aebi M
J Biol Chem 289 34953-64 (2014)
PMID: 25342741

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Extracellular membrane protein CFEM domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.09 KDa
Source organism: Coprinopsis cinerea
Expression system: Komagataella pastoris
UniProt:
  • Canonical: D6RKI7 (Residues: 129-186; Coverage: 11%)
Gene name: CC1G_13813
Sequence domains: Fungal defensin Copsin
Structure domains: Defensin A-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: simulated annealing
Expression system: Komagataella pastoris

Quick links

Citations

28 review citations

Antimicrobial peptides in 2014.
Wang et al. (2015)
27 more

1 mention without citation

Copsin, a novel peptide-based fungal antibiotic interfering with the peptidoglycan synthesis.
Essig et al. (2014)