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Structure paper

TitleProduct release rather than chelation determines metal specificity for ferrochelatase.
Journal, issue, pagesJ. Mol. Biol., Vol. 393, Page 308-319, Year 2009
Publish dateMay 6, 2009 (structure data deposition date)
AuthorsMedlock, A.E. / Carter, M. / Dailey, T.A. / Dailey, H.A. / Lanzilotta, W.N.
External linksJ. Mol. Biol. / PubMed:19703464
MethodsX-ray diffraction
Resolution1.6 - 2.2 Å
Structure data

PDB-3hcn:
Hg and protoporphyrin bound Human Ferrochelatase
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3hco:
Human ferrochelatase with Cd and protoporphyrin IX bound
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3hcp:
Human ferrochelatase with Mn and deuteroporphyrin bound
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3hcr:
Human Ferrochelatase with deuteroporphyrin and Ni Bound
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-CHD:
CHOLIC ACID

ChemComp-IMD:
IMIDAZOLE

ChemComp-BCT:
BICARBONATE ION

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FDE:
FE(III) DEUTEROPORPHYRIN IX

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLYASE / ferrochelatase / metal selectivity / Disease mutation / Heme biosynthesis / Iron / Iron-sulfur / Membrane / Metal-binding / Mitochondrion / Mitochondrion inner membrane / Porphyrin biosynthesis / Transit peptide

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