› 6evd

X-ray diffraction
1.19Å resolution

Structure of R173A A. niger Fdc1 with prFMN in the hydroxylated form

Released:
DOI: 10.2210/pdb6evd/pdb
PDB entry 6evd coloured by chain, front view.
PDB entry 6evd coloured by chain, side view.
PDB entry 6evd coloured by chain, top view.
Source organism: Aspergillus niger CBS 513.88
Primary publication:
The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.
Bailey SS, Payne KAP, Fisher K, Marshall SA, Cliff MJ, Spiess R, Parker DA, Rigby SEJ, Leys D
OpenAccess logo J Biol Chem 293 2272-2287 (2018)
PMID: 29259125

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferulic acid decarboxylase 1 Chain: A
Molecule details ›
Chain: A
Length: 508 amino acids
Theoretical weight: 56.25 KDa
Source organism: Aspergillus niger CBS 513.88
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A2QHE5 (Residues: 1-500; Coverage: 100%)
Gene names: An03g06590, fdc1
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand MN 1 x MN
Ligand K 1 x K
Ligand BYN 1 x BYN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21212
Unit cell:
a: 96.23Å b: 64.11Å c: 87.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.144 0.162
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Formation and Cleavage of C-C Bonds by Enzymatic Oxidation-Reduction Reactions.
Guengerich et al. (2018)
4 more

1 mention without citation

The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.
Bailey et al. (2018)