› 3d2h

X-ray diffraction
1.65Å resolution

Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal form

Released:
DOI: 10.2210/pdb3d2h/pdb
PDB entry 3d2h coloured by chain, front view.
PDB entry 3d2h coloured by chain, side view.
PDB entry 3d2h coloured by chain, top view.
Source organism: Eschscholzia californica
Primary publication:
A concerted mechanism for berberine bridge enzyme.
Winkler A, Lyskowski A, Riedl S, Puhl M, Kutchan TM, Macheroux P, Gruber K
Nat Chem Biol 4 739-41 (2008)
PMID: 18953357

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: 538 amino acids
Theoretical weight: 60.05 KDa
Source organism: Eschscholzia californica
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P30986 (Residues: 1-21, 24-538; Coverage: 100%)
Gene name: BBE1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand FSH 1 x FSH
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: C2
Unit cell:
a: 99.913Å b: 94.842Å c: 63.977Å
α: 90° β: 100.31° γ: 90°
R-values:
R R work R free
0.155 0.155 0.186
Expression system: Komagataella pastoris

Quick links

Citations

20 review citations

Benzylisoquinoline alkaloid metabolism: a century of discovery and a brave new world.
Hagel et al. (2013)
19 more

5 mentions without citation

Harnessing ortho-Quinone Methides in Natural Product Biosynthesis and Biocatalysis.
Purdy et al. (2022)
4 more