› 2hre

X-ray diffraction
2.5Å resolution

Structure of human ferrochelatase variant E343K with protoporphyrin IX bound

Released:
DOI: 10.2210/pdb2hre/pdb
PDB entry 2hre coloured by chain, front view.
PDB entry 2hre coloured by chain, side view.
PDB entry 2hre coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substrate interactions with human ferrochelatase.
Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN
Proc Natl Acad Sci U S A 104 1789-93 (2007)
PMID: 17261801

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-149809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferrochelatase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 359 amino acids
Theoretical weight: 41.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22830 (Residues: 65-423; Coverage: 85%)
Gene name: FECH
Sequence domains: Ferrochelatase
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand PP9 6 x PP9
Ligand FES 4 x FES
Ligand CHD 2 x CHD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 61.952Å b: 88.388Å c: 93.253Å
α: 102.41° β: 109.34° γ: 105.58°
R-values:
R R work R free
0.216 0.216 0.279
Expression system: Escherichia coli

Quick links

Citations

16 review citations

The biochemistry of heme biosynthesis.
Heinemann et al. (2008)
15 more

8 mentions without citation

Substrate interactions with human ferrochelatase.
Medlock et al. (2007)
7 more