X-ray diffraction
2.2Å resolution

2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound


Function and Biology Details

Reaction catalysed:
Protoheme + 2 H(+) = protoporphyrin + Fe(2+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

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

Ligands and Environments

Cofactor: Ligand PP9 6 x PP9
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 61.893Å b: 88.454Å c: 93.1Å
α: 102.49° β: 108.99° γ: 105.55°
R R work R free
0.222 0.222 0.261
Expression system: Escherichia coli