› 2qd5

X-ray diffraction
2.3Å resolution

Structure of wild type human ferrochelatase in complex with a lead-porphyrin compound

Released:
DOI: 10.2210/pdb2qd5/pdb
PDB entry 2qd5 coloured by chain, front view.
PDB entry 2qd5 coloured by chain, side view.
PDB entry 2qd5 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:
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: 41.18 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

7 bound ligands:
Ligand PB 2 x PB
Ligand FES 2 x FES
Ligand CHD 4 x CHD
Ligand PP9 2 x PP9
Ligand GOL 1 x GOL
Ligand ACY 3 x ACY
Ligand OXY 1 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 86.218Å b: 92.811Å c: 109.808Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.28
Expression system: Escherichia coli

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Citations

11 review citations

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

1 mention without citation

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.
Medlock et al. (2007)