X-ray diffraction
2.2Å resolution

Crystal structure of human ferrochelatase mutant with His 341 replaced by Cys


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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Ferrochelatase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 41.07 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 94.049Å b: 87.608Å c: 110.632Å
α: 90° β: 90° γ: 90°
R R work R free
0.21 0.21 0.245
Expression system: Escherichia coli