› 3hcn

X-ray diffraction
1.6Å resolution

Hg and protoporphyrin bound Human Ferrochelatase

Released:
DOI: 10.2210/pdb3hcn/pdb
PDB entry 3hcn coloured by chain, front view.
PDB entry 3hcn coloured by chain, side view.
PDB entry 3hcn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Product release rather than chelation determines metal specificity for ferrochelatase.
Medlock AE, Carter M, Dailey TA, Dailey HA, Lanzilotta WN
J Mol Biol 393 308-19 (2009)
PMID: 19703464

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferrochelatase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 41.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22830 (Residues: 65-423; Coverage: 85%)
Gene name: FECH
Sequence domains: Ferrochelatase
Structure domains: Rossmann fold

Ligands and Environments

7 bound ligands:
Ligand FES 2 x FES
Ligand CHD 4 x CHD
Ligand IMD 3 x IMD
Ligand BCT 1 x BCT
Ligand HEM 2 x HEM
Ligand SO4 2 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 86.479Å b: 92.964Å c: 109.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.236
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structure and function of enzymes in heme biosynthesis.
Layer et al. (2010)
10 more

3 mentions without citation

Product release rather than chelation determines metal specificity for ferrochelatase.
Medlock et al. (2009)
2 more