› › Structure analysis

THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.

X-ray diffraction
2.35Å resolution
PDB entry 1qgh coloured by chain, front view.
PDB entry 1qgh coloured by chain, side view.
PDB entry 1qgh coloured by chain, top view.
Source organism: Listeria innocua
Assembly composition:
homo dodecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

Quick links

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Assembly Name: DNA protection during starvation protein
hide full assembly name
Multimeric state: homo dodecamer
Accessible surface area: 60822.64 Å2
Buried surface area: 38485.41 Å2
Dissociation area: 11,203.92 Å2
Dissociation energy (ΔGdiss): 115.53 kcal/mol
Dissociation entropy (TΔSdiss): 70.8 kcal/mol
Symmetry number: 12
PDBe Complex ID: PDB-CPX-160451

Macromolecules

DNA protection during starvation protein
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 156 amino acids
Theoretical weight: 18.07 KDa
Source organism: Listeria innocua
UniProt:
  • Canonical: P80725 (Residues: 1-156; Coverage: 100%)
Gene names: dps, flp, fri, lin0942
Pfam: Ferritin-like domain
InterPro:
CATH: Ferritin
SCOP: Ferritin
DNA protection during starvation protein in PDB entry 1qgh, assembly 1, front view.
DNA protection during starvation protein in PDB entry 1qgh, assembly 1, side view.
DNA protection during starvation protein in PDB entry 1qgh, assembly 1, top view.
Molecule details ›

Search similar proteins

Quick links