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TitleA pi-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase.
Journal, issue, pagesJ. Mol. Biol., Vol. 373, Page 1006-1016, Year 2007
Publish dateJun 20, 2007 (structure data deposition date)
AuthorsMedlock, A.E. / Dailey, T.A. / Ross, T.A. / Dailey, H.A. / Lanzilotta, W.N.
External linksJ. Mol. Biol. / PubMed:17884090
MethodsX-ray diffraction
Resolution2 - 2.3 Å
Structure data

PDB-2qd1:
2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2qd2:
F110A variant of human ferrochelatase with protoheme bound
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2qd3:
Wild type human ferrochelatase crystallized with ammonium sulfate
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2qd4:
Wild type human ferrochelatase crystallized with MnCl2
Method: X-RAY DIFFRACTION / Resolution: 2.0 Å

PDB-2qd5:
Structure of wild type human ferrochelatase in complex with a lead-porphyrin compound
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-PP9:
PROTOPORPHYRIN IX

ChemComp-CHD:
CHOLIC ACID

ChemComp-IMD:
IMIDAZOLE

ChemComp-HOH:
WATER

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-PB:
LEAD (II) ION

ChemComp-ACY:
ACETIC ACID

ChemComp-OXY:
OXYGEN MOLECULE

Source
  • homo sapiens (human)
KeywordsLYASE / Ferrochelatase / heme biosynthesis / protopophyrin IX / BIOSYNTHETIC PROTEIN / Heme synthesis / Protoporphyrin IX / Iron / Porphyrin biosynthesis

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