› 1r3y

X-ray diffraction
1.76Å resolution

Uroporphyrinogen Decarboxylase in complex with coproporphyrinogen-III

Released:
DOI: 10.2210/pdb1r3y/pdb
PDB entry 1r3y coloured by chain, front view.
PDB entry 1r3y coloured by chain, side view.
PDB entry 1r3y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase.
Phillips JD, Whitby FG, Kushner JP, Hill CP
EMBO J 22 6225-33 (2003)
PMID: 14633982

Function and Biology Details

Reaction catalysed: 
Uroporphyrinogen III = coproporphyrinogen + 4 CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uroporphyrinogen decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 40.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06132 (Residues: 1-367; Coverage: 100%)
Gene name: UROD
Sequence domains: Uroporphyrinogen decarboxylase (URO-D)
Structure domains: TIM Barrel

Ligands and Environments

1 bound ligand:
Ligand CP3 1 x CP3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P3121
Unit cell:
a: 103.14Å b: 103.14Å c: 74.56Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.158 0.186
Expression system: Escherichia coli

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Citations

12 review citations

Biosynthesis of heme in mammals.
Ajioka et al. (2006)
11 more

3 mentions without citation

Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase.
Phillips et al. (2003)
2 more