PDBe 1hrk

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE

Released:
Source organism: Homo sapiens

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
Macromolecule:
Ferrochelatase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 41.13 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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, null
Spacegroup: P212121
Unit cell:
a: 93.433Å b: 87.569Å c: 109.699Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.226
Expression system: Escherichia coli