1qgh

X-ray diffraction
2.35Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA protection during starvation protein Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
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
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 87.54Å b: 137.5Å c: 173.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 not available