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Structure paper

TitleFerroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity.
Journal, issue, pagesChemistry, Vol. 22, Page 16213-16219, Year 2016
Publish dateApr 8, 2016 (structure data deposition date)
AuthorsBernacchioni, C. / Pozzi, C. / Di Pisa, F. / Mangani, S. / Turano, P.
External linksChemistry / PubMed:27650996
MethodsX-ray diffraction
Resolution1.1 - 1.5 Å
Structure data

PDB-5j8s:
Iron-free state of Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-5j8w:
One minute iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
Method: X-RAY DIFFRACTION / Resolution: 1.11 Å

PDB-5j93:
Five minutes iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-5j9v:
Ten minutes iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

PDB-5jac:
Sixty minutes iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
Method: X-RAY DIFFRACTION / Resolution: 1.18 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FE2:
Unknown entry

Source
  • lithobates catesbeiana (American bullfrog)
KeywordsOXIDOREDUCTASE / Rana Catesbeiana / ferritin variant / ferroxidase activity / M type / H' type / oxidoreductase activity / iron

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