› 2qd1

X-ray diffraction
2.2Å resolution

2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound

Released:
DOI: 10.2210/pdb2qd1/pdb
PDB entry 2qd1 coloured by chain, front view.
PDB entry 2qd1 coloured by chain, side view.
PDB entry 2qd1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.
Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN
J Mol Biol 373 1006-16 (2007)
PMID: 17884090

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149808 (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

4 bound ligands:
Ligand FES 4 x FES
Ligand PP9 6 x PP9
Ligand CHD 2 x CHD
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 61.893Å b: 88.454Å c: 93.1Å
α: 102.49° β: 108.99° γ: 105.55°
R-values:
R R work R free
0.222 0.222 0.261
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

14 mentions without citation

One ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoans.
Hamza et al. (2012)
13 more