PDBe 2aex

X-ray diffraction
1.58Å resolution

The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary Coproporphyria

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of hereditary coproporphyria.
Proc. Natl. Acad. Sci. U.S.A. 102 14232-7 (2005)
PMID: 16176984

Function and Biology Details

Reaction catalysed:
Coproporphyrinogen-III + O(2) + 2 H(+) = protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 39.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36551 (Residues: 111-454; Coverage: 76%)
Gene names: CPO, CPOX, CPX
Sequence domains: Coproporphyrinogen III oxidase
Structure domains: Coproporphyrinogen III oxidase, aerobic

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P23
Unit cell:
a: 112.741Å b: 112.741Å c: 112.741Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.208
Expression system: Escherichia coli BL21(DE3)