› 1ak1

X-ray diffraction
1.9Å resolution

FERROCHELATASE FROM BACILLUS SUBTILIS

Released:
DOI: 10.2210/pdb1ak1/pdb
PDB entry 1ak1 coloured by chain, front view.
PDB entry 1ak1 coloured by chain, side view.
PDB entry 1ak1 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis.
Al-Karadaghi S, Hansson M, Nikonov S, Jönsson B, Hederstedt L
Structure 5 1501-10 (1997)
PMID: 9384565

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 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 49.39Å b: 50.19Å c: 120.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

20 review citations

Tetrapyrrole biosynthesis in higher plants.
Tanaka et al. (2007)
19 more

8 mentions without citation

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