X-ray diffraction
2.9Å resolution

Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of the catalytic site

Source organism: Vitis vinifera

Function and Biology Details

Reactions catalysed:
A (2R,3S,4S)-leucoanthocyanidin + NADP(+) = a (2R,3R)-dihydroflavonol + NADPH
(2S)-flavan-4-ol + NADP(+) = (2S)-flavanone + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydroflavonol 4-reductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 337 amino acids
Theoretical weight: 37.69 KDa
Source organism: Vitis vinifera
Expression system: Escherichia coli
  • Canonical: P51110 (Residues: 1-337; Coverage: 100%)
Gene name: DFR
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

Cofactor: Ligand NAP 6 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P6122
Unit cell:
a: 174.943Å b: 174.943Å c: 290.167Å
α: 90° β: 90° γ: 120°
R R work R free
0.292 0.288 0.366
Expression system: Escherichia coli