Magnesium in PDB 6fw8: Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 5-Methyl-L-Tryptophan

All present enzymatic activity of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 5-Methyl-L-Tryptophan:
1.4.3.23;

The structure of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 5-Methyl-L-Tryptophan, PDB code: 6fw8 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)	58.88 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	151.130, 174.088, 93.922, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 24.6

The binding sites of Magnesium atom in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 5-Methyl-L-Tryptophan (pdb code 6fw8). 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 5-Methyl-L-Tryptophan, PDB code: 6fw8:
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 5-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 5-Methyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:55.6 occ:1.00 O1P B:FAD501 2.7 43.1 1.0 O B:ALA240 2.9 48.6 1.0 N B:GLY13 2.9 36.9 1.0 N B:GLY16 3.0 47.5 1.0 CA B:GLY13 3.2 41.4 1.0 C B:GLY13 3.5 45.9 1.0 O5B B:FAD501 3.7 42.5 1.0 CB B:ALA240 3.7 48.9 1.0 CB B:SER15 3.7 42.2 1.0 CA B:GLY16 3.7 38.9 1.0 C B:GLY11 3.7 44.5 1.0 O B:GLY13 3.8 37.1 1.0 N B:SER15 3.8 40.3 1.0 C B:ALA240 3.8 51.0 1.0 O B:GLY11 3.9 46.2 1.0 C5B B:FAD501 3.9 38.1 1.0 P B:FAD501 3.9 46.1 1.0 C B:SER15 4.0 49.7 1.0 N B:ALA12 4.0 39.2 1.0 C B:ALA12 4.0 35.9 1.0 CA B:SER15 4.0 46.6 1.0 C4B B:FAD501 4.0 45.8 1.0 CA B:GLY11 4.1 42.2 1.0 N B:ILE14 4.2 45.6 1.0 O3P B:FAD501 4.2 51.2 1.0 CA B:ALA12 4.4 38.3 1.0 CA B:ALA240 4.4 45.1 1.0 OG B:SER15 4.5 48.5 1.0 O2P B:FAD501 4.6 55.3 1.0 PA B:FAD501 4.6 39.5 1.0 O4B B:FAD501 4.6 44.2 1.0 C B:ILE14 4.7 45.5 1.0 C B:GLY16 4.9 47.1 1.0 N B:ILE241 4.9 46.7 1.0 N B:LEU17 5.0 38.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 5-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 5-Methyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:41.4 occ:0.70 O A:ALA240 2.6 46.1 1.0 O1P A:FAD501 2.8 42.2 1.0 N A:GLY16 2.9 42.2 1.0 N A:GLY13 3.1 42.6 1.0 CA A:GLY13 3.5 38.3 1.0 CB A:ALA240 3.5 39.2 1.0 CA A:GLY16 3.6 34.3 1.0 C A:GLY11 3.6 42.6 1.0 O A:GLY11 3.6 43.3 1.0 C A:ALA240 3.7 53.2 1.0 C A:GLY13 3.7 44.7 1.0 CB A:SER15 3.7 39.8 1.0 C5B A:FAD501 3.8 44.2 1.0 O5B A:FAD501 3.9 44.7 1.0 O A:GLY13 3.9 38.2 1.0 N A:SER15 3.9 39.7 1.0 C A:SER15 3.9 52.4 1.0 N A:ALA12 3.9 43.4 1.0 P A:FAD501 4.0 41.8 1.0 CA A:SER15 4.0 38.9 1.0 CA A:GLY11 4.1 43.5 1.0 C4B A:FAD501 4.1 48.4 1.0 C A:ALA12 4.2 40.0 1.0 CA A:ALA240 4.2 44.1 1.0 O3P A:FAD501 4.3 45.8 1.0 CA A:ALA12 4.4 37.2 1.0 N A:ILE14 4.4 40.5 1.0 O2P A:FAD501 4.6 47.7 1.0 O4B A:FAD501 4.6 48.1 1.0 O A:HOH640 4.6 54.8 1.0 OG A:SER15 4.7 43.5 1.0 PA A:FAD501 4.8 43.3 1.0 N A:ILE241 4.8 43.4 1.0 C A:ILE14 4.8 43.2 1.0 C A:GLY16 4.9 41.9 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