› 4ec3

X-ray diffraction
2.65Å resolution

Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline

Released:
DOI: 10.2210/pdb4ec3/pdb
PDB entry 4ec3 coloured by chain, front view.
PDB entry 4ec3 coloured by chain, side view.
PDB entry 4ec3 coloured by chain, top view.
Source organism: Eschscholzia californica
Primary publication:
Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme.
Wallner S, Winkler A, Riedl S, Dully C, Horvath S, Gruber K, Macheroux P
Biochemistry 51 6139-47 (2012)
PMID: 22757961

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: 57.81 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, MAN
Carbohydrate polymer
3 bound ligands:
Ligand REN 1 x REN
Ligand NAG 1 x NAG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 98.763Å b: 92.943Å c: 63.579Å
α: 90° β: 100.31° γ: 90°
R-values:
R R work R free
0.183 0.18 0.235
Expression system: Komagataella pastoris

Quick links

Citations

2 review citations

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

1 mention without citation

Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme.
Wallner et al. (2012)