EC Number   |
|---|
    1.16.3.1 | - |
| 1.16.3.1 | crystal structure analysis, PDB ID 1TJO |
| 1.16.3.1 | crystal structure analysis, PDB ID 3DKT |
| 1.16.3.1 | crystal structure analysis, PDB ID 4PT2 |
| 1.16.3.1 | crystal structure determination of the enzyme apo form and metal-ion bound forms, such as iron, zinc, and cadmium, of HP-NAP, structure analysis |
| 1.16.3.1 | crystal structures of iron-loaded frog M ferritin determined by flash freezing crystals soaked for different times in iron(II) solutions under aerobic conditions. These structures provide the first X-ray picture of iron(III) products at the ferroxidase site in higher eukaryotes ferritins |
| 1.16.3.1 | crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC), indicating that HP-NAP can store zinc and cadmium ions in addition to iron ions. Another zinc ion is found inside of the negatively-charged 3fold-related pore, as an iron ion in the iron-containing form, and therefore the pore is suitable for metal ions to pass through |
| 1.16.3.1 | determination of the crystal structure of Streptococcus pyogenes Dpr in iron-free and iron-bound form at 2.0 and 1.93 A resolution, respectively |
| 1.16.3.1 | determined at 3 A. The crystallographic data implicate the importance of the extended C-terminal region in the iron entry from the three-fold channels to the ferroxidase centre and making iron more readily accessible for the oxidation |
| 1.16.3.1 | hanging drop method, crystal structure of CueO at 1.1 A with the 45-residue methionine-rich segment fully resolved, revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a C-terminal highly mobile segment rich in methionine and histidine residues. Structures of CueO with a C500S mutation, and CueO with six methionines changed to serine |
