› 1c9e

X-ray diffraction
2.3Å resolution

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

Released:
DOI: 10.2210/pdb1c9e/pdb
PDB entry 1c9e coloured by chain, front view.
PDB entry 1c9e coloured by chain, side view.
PDB entry 1c9e coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural and mechanistic basis of porphyrin metallation by ferrochelatase.
Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S
J Mol Biol 297 221-32 (2000)
PMID: 10704318

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coproporphyrin III ferrochelatase Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 34.89 KDa
Source organism: Bacillus subtilis
Expression system: Bacteria
UniProt:
  • Canonical: P32396 (Residues: 5-310; Coverage: 99%)
Gene names: BSU10130, cpfC, hemF, hemH
Sequence domains: Ferrochelatase
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand MP1 1 x MP1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 49.84Å b: 58.56Å c: 98.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.255
Expression system: Bacteria

Quick links

Citations

3 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
2 more

3 mentions without citation

The Interplay of Glycosaminoglycans and Cysteine Cathepsins in Mucopolysaccharidosis.
David et al. (2023)
2 more