› 2h1w

X-ray diffraction
2.6Å resolution

Crystal structure of the His183Ala mutant variant of Bacillus subtilis ferrochelatase

Released:
DOI: 10.2210/pdb2h1w/pdb
PDB entry 2h1w coloured by chain, front view.
PDB entry 2h1w coloured by chain, side view.
PDB entry 2h1w coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX.
Hansson MD, Karlberg T, Rahardja MA, Al-Karadaghi S, Hansson M
Biochemistry 46 87-94 (2007)
PMID: 17198378

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-152294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coproporphyrin III ferrochelatase Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 35.32 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
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 FE2 1 x FE2
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P212121
Unit cell:
a: 47.94Å b: 49.72Å c: 116.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.259
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

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