X-ray diffraction
2.46Å resolution

Structure of C. dubliensis Fdc1 with the prenylated-flavin cofactor in the iminium form.


Function and Biology Details

Reaction catalysed:
4-coumarate = 4-vinylphenol + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Ferulic acid decarboxylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 513 amino acids
Theoretical weight: 57.74 KDa
Source organism: Candida dubliniensis
Expression system: Escherichia coli
  • Canonical: B9WJ66 (Residues: 1-513; Coverage: 100%)
Gene names: CD36_64160, FDC1
Sequence domains: 3-octaprenyl-4-hydroxybenzoate carboxy-lyase
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 91.97Å b: 64.55Å c: 96.05Å
α: 90° β: 91.07° γ: 90°
R R work R free
0.208 0.205 0.256
Expression system: Escherichia coli