› 3gsy

X-ray diffraction
1.63Å resolution

Structure of berberine bridge enzyme in complex with dehydroscoulerine

Released:
DOI: 10.2210/pdb3gsy/pdb
PDB entry 3gsy coloured by chain, front view.
PDB entry 3gsy coloured by chain, side view.
PDB entry 3gsy coloured by chain, top view.
Source organism: Eschscholzia californica
Primary publication:
Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine.
Winkler A, Puhl M, Weber H, Kutchan TM, Gruber K, Macheroux P
Phytochemistry 70 1092-1097 (2009)
PMID: 19570558

Function and Biology Details

Reaction catalysed: 
(S)-reticuline + O(2) = (S)-scoulerine + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Reticuline oxidase Chain: A
Molecule details ›
Chain: A
Length: 519 amino acids
Theoretical weight: 57.88 KDa
Source organism: Eschscholzia californica
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P30986 (Residues: 24-538; Coverage: 100%)
Gene name: BBE1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
3 bound ligands:
Ligand DEH 1 x DEH
Ligand NAG 1 x NAG
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P41212
Unit cell:
a: 68.94Å b: 68.94Å c: 247.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.162 0.185
Expression system: Komagataella pastoris

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Citations

2 review citations

Oxidative Cyclization in Natural Product Biosynthesis.
Tang et al. (2017)
1 more