› 2q3j

X-ray diffraction
2.39Å resolution

Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin

Released:
DOI: 10.2210/pdb2q3j/pdb
PDB entry 2q3j coloured by chain, front view.
PDB entry 2q3j coloured by chain, side view.
PDB entry 2q3j coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.
Karlberg T, Hansson MD, Yengo RK, Johansson R, Thorvaldsen HO, Ferreira GC, Hansson M, Al-Karadaghi S
J Mol Biol 378 1074-83 (2008)
PMID: 18423489

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-542704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coproporphyrin III ferrochelatase Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 35.19 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P32396 (Residues: 2-310; 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 H02 1 x H02
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-5
Spacegroup: P212121
Unit cell:
a: 49.78Å b: 58.57Å c: 97.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Structure and function of enzymes in heme biosynthesis.
Layer et al. (2010)
8 more

2 mentions without citation

Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.
Karlberg et al. (2008)
1 more