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

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Ligands and binding sites

• FAD · Flavin-adenine dinucleotide · ligand · chains A
• FSH · (2R,3S,4S)-5-[(4R)-6',7'-dimethyl-2,3',5-trioxo-1'H-spiro[imidazolidine-4,2'-quinoxalin]-4'(3'H)-yl]-2,3,4-trihydroxypentyl-adenosine diphosphate · ligand · chains A
• MAN · alpha-D-mannopyranose · sugar · 4 copies
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 2 cofactor, 2 covalent, 2 glycan, 1 disulfide (flavinylation, covalent ligand, N-glycosylation, disulfide).

Compared structures

• 3D2H · Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal… · the same entry in another collection · chain A against A, TM-score 1.00
• P30986 · AlphaFold monomer V2.0 prediction for reticuline oxidase (P30986) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P30986
• Elsewhere: RCSB PDB 3D2H · PDBe 3D2H · UniProt P30986