Magnesium in PDB 6fwa: Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan

All present enzymatic activity of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan:
1.4.3.23;

The structure of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan, PDB code: 6fwa was solved by H.E.Lai, M.Morgan, S.Moore, P.Freemont, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.13 / 2.85
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	151.344, 172.418, 94.269, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 31.6

The binding sites of Magnesium atom in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan (pdb code 6fwa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan, PDB code: 6fwa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:55.1 occ:1.00 N B:GLY13 2.7 45.9 1.0 O1P B:FAD501 2.8 45.1 1.0 N B:GLY16 3.0 47.8 1.0 O B:ALA240 3.0 41.1 1.0 CA B:GLY13 3.2 36.8 1.0 O B:GLY13 3.2 38.0 1.0 C B:GLY13 3.3 48.0 1.0 OG B:SER15 3.4 60.0 1.0 CA B:GLY16 3.5 46.5 1.0 C B:GLY11 3.6 37.0 1.0 N B:ALA12 3.7 39.7 1.0 O5B B:FAD501 3.7 43.9 1.0 O B:GLY11 3.8 41.1 1.0 C B:ALA12 3.8 53.2 1.0 C5B B:FAD501 4.0 48.4 1.0 P B:FAD501 4.0 53.6 1.0 C4B B:FAD501 4.0 48.2 1.0 CA B:ALA12 4.0 39.8 1.0 N B:SER15 4.0 39.1 1.0 CB B:ALA240 4.1 37.8 1.0 C B:SER15 4.1 43.9 1.0 N B:ILE14 4.1 51.5 1.0 C B:ALA240 4.1 47.3 1.0 CA B:GLY11 4.2 40.1 1.0 O2P B:FAD501 4.3 58.0 1.0 O3P B:FAD501 4.4 58.6 1.0 CA B:SER15 4.4 42.8 1.0 CB B:SER15 4.5 54.2 1.0 O4B B:FAD501 4.5 42.5 1.0 C B:GLY16 4.7 42.4 1.0 PA B:FAD501 4.7 46.6 1.0 C B:ILE14 4.7 45.6 1.0 CA B:ALA240 4.7 49.3 1.0 N B:LEU17 4.8 45.0 1.0 O B:ALA12 4.9 56.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 7-Methyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:59.0 occ:1.00 O A:ALA240 2.3 42.7 1.0 N A:GLY13 2.8 43.6 1.0 CA A:GLY13 3.0 48.3 1.0 O1P A:FAD501 3.1 37.8 1.0 N A:GLY16 3.2 43.8 1.0 CB A:ALA240 3.4 52.6 1.0 C A:ALA240 3.5 46.1 1.0 C A:GLY13 3.5 51.6 1.0 O A:GLY13 3.6 43.4 1.0 C5B A:FAD501 3.6 44.0 1.0 C A:GLY11 3.7 51.1 1.0 O3P A:FAD501 3.8 50.0 1.0 O A:GLY11 3.8 57.6 1.0 CA A:GLY16 3.9 37.2 1.0 C4B A:FAD501 3.9 52.4 1.0 CB A:SER15 3.9 39.9 1.0 C A:ALA12 4.0 50.8 1.0 CA A:GLY11 4.0 46.3 1.0 N A:ALA12 4.0 41.5 1.0 O5B A:FAD501 4.0 38.6 1.0 P A:FAD501 4.0 48.0 1.0 CA A:ALA240 4.0 49.5 1.0 N A:SER15 4.3 46.1 1.0 C A:SER15 4.3 48.0 1.0 O4B A:FAD501 4.3 58.0 1.0 N A:ILE14 4.4 44.1 1.0 CA A:ALA12 4.4 42.1 1.0 CA A:SER15 4.4 36.2 1.0 N A:ILE241 4.6 43.5 1.0 PA A:FAD501 4.6 47.0 1.0 O2P A:FAD501 4.7 45.8 1.0 OG A:SER15 4.7 56.4 1.0 O A:HOH617 4.8 47.7 1.0 CA A:ILE241 4.9 48.7 1.0 O A:ALA12 5.0 46.8 1.0

H.E.Lai, A.M.C.Obled, S.M.Chee, R.M.Morgan, S.V.Sharma, S.J.Moore, K.M.Polizzi, R.J.M.Goss, P.S.Freemont. A Genochemetic Strategy For Derivatization of the Violacein Natural Product Scaffold Biorxiv 2019.
DOI: 10.1101/202523