Magnesium in PDB 3fwa: Structure of Berberine Bridge Enzyme, C166A Variant in Complex with (S)-Reticuline

All present enzymatic activity of Structure of Berberine Bridge Enzyme, C166A Variant in Complex with (S)-Reticuline:
1.21.3.3;

The structure of Structure of Berberine Bridge Enzyme, C166A Variant in Complex with (S)-Reticuline, PDB code: 3fwa 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)	41.89 / 1.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.870, 68.870, 246.460, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 17.7

The binding sites of Magnesium atom in the Structure of Berberine Bridge Enzyme, C166A Variant in Complex with (S)-Reticuline (pdb code 3fwa). 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, C166A Variant in Complex with (S)-Reticuline, PDB code: 3fwa:

Magnesium binding site 1 out of 1 in the Structure of Berberine Bridge Enzyme, C166A Variant in Complex with (S)-Reticuline


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, C166A Variant in Complex with (S)-Reticuline within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg526 b:44.5 occ:1.00 O A:HOH565 1.8 38.1 1.0 O A:HOH4 1.9 38.2 1.0 O A:HOH573 2.0 52.6 1.0 O A:HOH5 2.2 36.1 1.0 OD1 A:ASP45 2.4 35.0 1.0 OD1 A:ASP47 2.6 80.6 1.0 CG A:ASP47 3.2 75.6 1.0 CG A:ASP45 3.3 26.6 1.0 OD2 A:ASP45 3.4 24.5 1.0 CB A:ASP47 3.6 61.8 1.0 OD2 A:ASP47 4.0 80.6 1.0 N A:ASP47 4.3 44.4 1.0 CA A:ASP47 4.6 42.0 1.0 CB A:ASP45 4.7 37.2 1.0 OG A:SER46 4.9 73.4 1.0 N A:SER46 5.0 55.8 1.0

A.Winkler, K.Motz, S.Riedl, M.Puhl, P.Macheroux, K.Gruber. Structural Roles of Biocovalent Flaninylation in Berberine Bridge Enzyme To Be Published.