X-ray diffraction
2.35Å resolution

Crystal structure of human ferrochelatase mutant with Phe 337 replaced by Ala

Source organism: Homo sapiens
Entry authors: Dailey HA, Wu C-K, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose JP

Function and Biology Details

Reaction catalysed:
Protoheme + 2 H(+) = protoporphyrin + Fe(2+)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
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: 41.06 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: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 86.686Å b: 94.052Å c: 113.276Å
α: 90° β: 90° γ: 90°
R R work R free
0.195 0.192 0.253
Expression system: Escherichia coli