X-ray diffraction
2.4Å resolution

Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.

Source organism: Escherichia coli K-12
Primary publication:
Structural basis for iron mineralization by bacterioferritin.
J. Am. Chem. Soc. 131 6808-13 (2009)
PMID: 19391621

Function and Biology Details

Reaction catalysed:
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Bacterioferritin 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: 158 amino acids
Theoretical weight: 18.52 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P0ABD3 (Residues: 1-158; Coverage: 100%)
Gene names: JW3298, b3336, bfr
Structure domains: Ferritin

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P42212
Unit cell:
a: 207.397Å b: 207.397Å c: 142.451Å
α: 90° β: 90° γ: 90°
R R work R free
0.241 0.24 0.26
Expression system: Escherichia coli