› 1c1h

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN

Released:
DOI: 10.2210/pdb1c1h/pdb
PDB entry 1c1h coloured by chain, front view.
PDB entry 1c1h coloured by chain, side view.
PDB entry 1c1h 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: 310 amino acids
Theoretical weight: 35.39 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P32396 (Residues: 1-310; Coverage: 100%)
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 MMP 1 x MMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 49.97Å b: 58.68Å c: 98.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.231
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Recent overview of the Mg branch of the tetrapyrrole biosynthesis leading to chlorophylls.
Masuda T. (2008)
1 more

12 mentions without citation

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