X-ray diffraction
1.35Å resolution

Crystal Structure of Candida glabrata FMN Adenylyltransferase in complex with FAD and Inorganic Pyrophosphate

Source organism: [Candida] glabrata
Primary publication:
Structure and mechanism of a eukaryotic FMN adenylyltransferase.
J. Mol. Biol. 389 388-400 (2009)
PMID: 19375431

Function and Biology Details

Reaction catalysed:
ATP + FMN = diphosphate + FAD
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
PAPS_reduct domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 308 amino acids
Theoretical weight: 35.99 KDa
Source organism: [Candida] glabrata
Expression system: Escherichia coli
  • Canonical: Q6FNA9 (Residues: 1-304; Coverage: 100%)
Gene names: CAGL0K01397g, FMNAT
Sequence domains: Phosphoadenosine phosphosulfate reductase family
Structure domains: HUPs

Ligands and Environments

Cofactor: Ligand FAD 6 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 206.583Å b: 81.481Å c: 136.603Å
α: 90° β: 129.79° γ: 90°
R R work R free
0.155 0.153 0.187
Expression system: Escherichia coli