Structure analysis

Crystal Structure Of Uroporphyrinogen Decarboxylase From Aquifex aeolicus

X-ray diffraction
1.9Å resolution
Source organism: Aquifex aeolicus
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 25286.46 Å2
Buried surface area: 2309.74 Å2
Dissociation area: 1,056.07 Å2
Dissociation energy (ΔGdiss): 0.24 kcal/mol
Dissociation entropy (TΔSdiss): 13.76 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-130364

Macromolecules

Chains: A, B
Length: 338 amino acids
Theoretical weight: 38.73 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66667 (Residues: 1-338; Coverage: 100%)
Gene names: aq_334, hemE
Pfam: Uroporphyrinogen decarboxylase (URO-D)
InterPro:
CATH: TIM Barrel

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