› 5fo0

X-ray diffraction
2.51Å resolution

Function and Biology Details

Reactions catalysed: 
ATP + riboflavin = ADP + FMN
ATP + FMN = diphosphate + FAD
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176787 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional riboflavin kinase/FMN adenylyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 36.9 KDa
Source organism: Corynebacterium ammoniagenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q59263 (Residues: 1-338; Coverage: 100%)
Gene name: ribF
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PPV 2 x PPV
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P213
Unit cell:
a: 133.179Å b: 133.179Å c: 133.179Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.251
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Production of riboflavin and related cofactors by biotechnological processes.
Liu et al. (2020)
9 other articles

1 mention without citation

The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes.
Serrano et al. (2017)