Magnesium in PDB 3gsy: Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine

All present enzymatic activity of Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine:
1.21.3.3;

The structure of Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine, PDB code: 3gsy was solved by A.Winkler, P.Macheroux, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.35 / 1.63
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.940, 68.940, 247.260, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 18.5

The binding sites of Magnesium atom in the Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine (pdb code 3gsy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine, PDB code: 3gsy:

Magnesium binding site 1 out of 1 in the Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Berberine Bridge Enzyme in Complex with Dehydroscoulerine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg542 b:47.3 occ:1.00 O A:HOH574 2.1 48.1 1.0 OD1 A:ASP47 2.1 75.0 1.0 O A:HOH543 2.1 39.3 1.0 O A:HOH5 2.1 30.0 1.0 OD1 A:ASP45 2.4 46.2 1.0 O A:HOH4 2.5 60.2 1.0 CG A:ASP47 3.1 73.6 1.0 CG A:ASP45 3.3 40.2 1.0 OD2 A:ASP45 3.4 30.7 1.0 OD2 A:ASP47 3.5 78.1 1.0 O A:HOH609 3.6 54.3 1.0 N A:ASP47 4.2 60.6 1.0 CB A:ASP47 4.5 65.2 1.0 CB A:ASP45 4.7 43.9 1.0 CA A:ASP47 4.7 54.8 1.0 N A:SER46 4.8 75.3 1.0 C A:ASP47 4.9 39.4 1.0

A.Winkler, M.Puhl, H.Weber, T.M.Kutchan, K.Gruber, P.Macheroux. Berberine Bridge Enzyme Catalyzes the Six Electron Oxidation of (S)-Reticuline to Dehydroscoulerine. Phytochemistry V. 70 1092 2009.
ISSN: ISSN 0031-9422
PubMed: 19570558
DOI: 10.1016/J.PHYTOCHEM.2009.06.005