› 2pnj

X-ray diffraction
2.35Å resolution

Crystal structure of human ferrochelatase mutant with Phe 337 replaced by Ala

Released:
DOI: 10.2210/pdb2pnj/pdb
PDB entry 2pnj coloured by chain, front view.
PDB entry 2pnj coloured by chain, side view.
PDB entry 2pnj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.
Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J
Biochemistry 46 7973-9 (2007)
PMID: 17567154

Function and Biology Details

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

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: 41.06 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 86.686Å b: 94.052Å c: 113.276Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.253
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

1 mention without citation

Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.
Dailey et al. (2007)