› 5lg8

X-ray diffraction
1.98Å resolution

Human L-type ferritin iron loaded for 60 minutes

Released:
DOI: 10.2210/pdb5lg8/pdb
PDB entry 5lg8 coloured by chain, front view.
PDB entry 5lg8 coloured by chain, side view.
PDB entry 5lg8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (μ3-oxo)Tris[(μ2-peroxo)] triiron(III) cluster.
Pozzi C, Ciambellotti S, Bernacchioni C, Di Pisa F, Mangani S, Turano P
Proc Natl Acad Sci U S A 114 2580-2585 (2017)
PMID: 28202724

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferritin light chain Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 20.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P02792 (Residues: 1-175; Coverage: 100%)
Gene name: FTL
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

5 bound ligands:
Ligand CD 8 x CD
Ligand FE 4 x FE
Ligand OXY 1 x OXY
Ligand PER 3 x PER
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: I432
Unit cell:
a: 151.42Å b: 151.42Å c: 151.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 0.142 0.177
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Redox-Active Metal Ions and Amyloid-Degrading Enzymes in Alzheimer's Disease.
Kim et al. (2021)
3 more

5 mentions without citation

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