1z6o

X-ray diffraction
1.91Å resolution

Crystal Structure of Trichoplusia ni secreted ferritin

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero 24-mer (preferred)
PDBe Complex ID:
PDB-CPX-228012 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ferritin light 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: 212 amino acids
Theoretical weight: 24.34 KDa
Source organism: Trichoplusia ni
UniProt:
  • Canonical: A0A7E5WUT2 (Residues: 20-231; Coverage: 100%)
Gene names: Fer2LCH, LOC113505693
Sequence domains: Ferritin-like domain
Structure domains: Ferritin
Ferritin heavy chain Chains: M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: M, N, O, P, Q, R, S, T, U, V, W, X
Length: 191 amino acids
Theoretical weight: 21.8 KDa
Source organism: Trichoplusia ni
UniProt:
  • Canonical: A0A7E5WTY7 (Residues: 21-211; Coverage: 100%)
Gene names: Fer1HCH, LOC113505694
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: C2
Unit cell:
a: 206.88Å b: 145.697Å c: 209.158Å
α: 90° β: 94.93° γ: 90°
R-values:
R R work R free
0.189 0.189 0.194