PDBe 3erz

X-ray diffraction
3.06Å resolution

Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. Mercury Ions on the Three-Fold Channel

Released:

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:
Ferritin heavy chain 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: 183 amino acids
Theoretical weight: 21.14 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02794 (Residues: 1-183; Coverage: 100%)
Gene names: FTH, FTH1, FTHL6, OK/SW-cl.84, PIG15
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P4212
Unit cell:
a: 170.941Å b: 170.941Å c: 190.144Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.256