› 2nnl

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb2nnl/pdb
PDB entry 2nnl coloured by chain, front view.
PDB entry 2nnl coloured by chain, side view.
PDB entry 2nnl coloured by chain, top view.
Source organism: Vitis vinifera
Entry authors: Petit P, Langlois D'Estaintot B, Granier T, Gallois B

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroflavonol 4-reductase Chains: D, F
Molecule details ›
Chains: D, F
Length: 337 amino acids
Theoretical weight: 37.69 KDa
Source organism: Vitis vinifera
Expression system: Escherichia coli
UniProt:
  • 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 2 x NAP
1 bound ligand:
Ligand ERD 2 x ERD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 87.825Å b: 90.143Å c: 93.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.242
Expression system: Escherichia coli

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