› 2hrc

X-ray diffraction
1.7Å resolution

1.7 angstrom structure of human ferrochelatase variant R115L

Released:
DOI: 10.2210/pdb2hrc/pdb
PDB entry 2hrc coloured by chain, front view.
PDB entry 2hrc coloured by chain, side view.
PDB entry 2hrc 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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferrochelatase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 41.13 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

5 bound ligands:
Ligand CL 2 x CL
Ligand FES 2 x FES
Ligand IMD 2 x IMD
Ligand CHD 6 x CHD
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 88.526Å b: 92.983Å c: 110.454Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.242
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

7 mentions without citation

Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria.
Obi et al. (2022)
6 more