5gaq

Electron Microscopy
3.14Å resolution

Cryo-EM structure of the Lysenin Pore

Released:

Function and Biology Details

Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo nonamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysenin Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 310 amino acids
Theoretical weight: 34.98 KDa
Source organism: Eisenia fetida
Expression system: Escherichia coli
UniProt:
  • Canonical: O18423 (Residues: 1-297; Coverage: 100%)
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.14Å
Relevant EMDB volumes: EMD-8015
Expression system: Escherichia coli