3m4z

X-ray diffraction
1.94Å resolution

Crystal Structure of B. subtilis ferrochelatase with Cobalt bound at the active site

Released:
Source organism: Bacillus subtilis
Entry authors: Soderberg CAG, Hansson MD, Sreekanth R, Al-Karadaghi S, Hansson M

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-152294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coproporphyrin III ferrochelatase Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 35.26 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P32396 (Residues: 2-310; Coverage: 100%)
Gene names: BSU10130, cpfC, hemF, hemH
Sequence domains: Ferrochelatase
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P212121
Unit cell:
a: 48.41Å b: 49.9Å c: 118.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.199
Expression system: Escherichia coli