› 1r3s

X-ray diffraction
1.65Å resolution

Uroporphyrinogen Decarboxylase single mutant D86G in complex with coproporphyrinogen-I

Released:
DOI: 10.2210/pdb1r3s/pdb
PDB entry 1r3s coloured by chain, front view.
PDB entry 1r3s coloured by chain, side view.
PDB entry 1r3s 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: 40.77 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 1CP 1 x 1CP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 102.947Å b: 102.947Å c: 72.585Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.163 0.19
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

3 mentions without citation

Spectrum of disease-causing mutations in protein secondary structures.
Khan et al. (2007)
2 more