3e1p

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.

Released:
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
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.241 0.24 0.26
Expression system: Escherichia coli