Brand  (β version)

PDB ID: 3HCR

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Ligands
Code Name Style Show Link
CHD Cholic acid PoSSuM
CL Chloride ion PoSSuM
FDE Fe(III) deuteroporphyrin ix PoSSuM
FES Fe2/s2 (inorganic) cluster PoSSuM
GOL Glycerol PoSSuM
IMD Imidazole PoSSuM
OXY Oxygen molecule PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
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Structure summary

Code : 3HCR   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Human Ferrochelatase with deuteroporphyrin and Ni Bound
Release Data : 2009-11-10
Compound :
mol_id molecule chains synonym
1 Ferrochelatase, mitochondrial A,B Protoheme ferro-lyase, Heme synthetase
ec: 4.99.1.1
fragment: UNP residues 65-423
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: FECH
Authors : Medlock, A.E., Dailey, H.A., Lanzilotta, W.N.
Keywords : Ferrochelatase, metal selectivity, Disease mutation, Heme biosynthesis, Iron, Iron-sulfur, Lyase, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, Porphyrin biosynthesis, Transit peptide
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

Product release rather than chelation determines metal specificity for ferrochelatase.

Medlock, A.E.,Carter, M.,Dailey, T.A.  et al.
(2009)  J.Mol.Biol.  393 : 308 - 319

PubMed: 19703464
DOI: 10.1016/j.jmb.2009.08.042

Reaction

Chain : A, B
UniProt : P22830 (HEMH_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
2 H(+) + heme b = Fe(2+) + protoporphyrin IX 4.98.1.1 PubMed:27599036, PubMed:8276824
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