3a68

X-ray diffraction
1.8Å resolution

Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferritin-4, chloroplastic Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 212 amino acids
Theoretical weight: 24.02 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q948P5 (Residues: 36-247; Coverage: 86%)
Structure domains: Ferritin

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21212
Unit cell:
a: 222.61Å b: 220.886Å c: 122.452Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.142 0.173
Expression system: Escherichia coli