› 6sv3

X-ray diffraction
1.64Å resolution

Function and Biology Details

Reaction catalysed: 
Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186951 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coproporphyrin III ferrochelatase Chain: A
Molecule details ›
Chain: A
Length: 311 amino acids
Theoretical weight: 35.63 KDa
Source organism: Listeria monocytogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8Y565 (Residues: 1-309; Coverage: 100%)
Gene names: cpfC, hemH, lmo2211
Sequence domains: Ferrochelatase

Ligands and Environments

2 bound ligands:
Ligand FEC 1 x FEC
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 37.47Å b: 68.14Å c: 62.91Å
α: 90° β: 103.06° γ: 90°
R-values:
R R work R free
0.173 0.171 0.201
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.
Hofbauer et al. (2021)
1 more

3 mentions without citation

Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.
Falb et al. (2023)
2 more