› 4lyx

X-ray diffraction
1.23Å resolution

five minutes iron loaded frog M ferritin

Released:
DOI: 10.2210/pdb4lyx/pdb
PDB entry 4lyx coloured by chain, front view.
PDB entry 4lyx coloured by chain, side view.
PDB entry 4lyx coloured by chain, top view.
Source organism: Lithobates catesbeianus
Primary publication:
Time-lapse anomalous X-ray diffraction shows how Fe(2+) substrate ions move through ferritin protein nanocages to oxidoreductase sites.
Pozzi C, Di Pisa F, Lalli D, Rosa C, Theil E, Turano P, Mangani S
Acta Crystallogr D Biol Crystallogr 71 941-53 (2015)
PMID: 25849404

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139760 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferritin, middle subunit Chain: A
Molecule details ›
Chain: A
Length: 176 amino acids
Theoretical weight: 20.62 KDa
Source organism: Lithobates catesbeianus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07798 (Residues: 1-176; Coverage: 100%)
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

3 bound ligands:
Ligand FE2 3 x FE2
Ligand MG 11 x MG
Ligand CL 12 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: F432
Unit cell:
a: 184.18Å b: 184.18Å c: 184.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 0.175
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.
Jasniewski et al. (2018)
4 more

1 mention without citation

Time-lapse anomalous X-ray diffraction shows how Fe(2+) substrate ions move through ferritin protein nanocages to oxidoreductase sites.
Pozzi et al. (2015)