Magnesium in PDB 6g2p: Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with L-Tryptophan

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

The structure of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with L-Tryptophan, PDB code: 6g2p 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)	76.05 / 2.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	152.092, 175.338, 94.436, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 22.5

The binding sites of Magnesium atom in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with L-Tryptophan (pdb code 6g2p). 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 L-Tryptophan, PDB code: 6g2p:
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 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 L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg504 b:38.7 occ:1.00 O1P B:FAD501 2.8 29.0 1.0 O B:ALA240 2.9 35.4 1.0 N B:GLY13 3.0 30.1 1.0 N B:GLY16 3.0 34.1 1.0 CA B:GLY13 3.3 30.2 1.0 C B:GLY13 3.6 34.0 1.0 O5B B:FAD501 3.7 32.8 1.0 C B:GLY11 3.7 33.2 1.0 CA B:GLY16 3.7 26.8 1.0 O B:GLY11 3.7 37.1 1.0 CB B:ALA240 3.7 31.6 1.0 O B:GLY13 3.8 33.4 1.0 CB B:SER15 3.8 28.7 1.0 C5B B:FAD501 3.9 29.4 1.0 C B:ALA240 3.9 40.8 1.0 N B:SER15 3.9 29.2 1.0 P B:FAD501 4.0 28.6 1.0 N B:ALA12 4.0 29.2 1.0 C B:SER15 4.0 35.3 1.0 CA B:GLY11 4.0 28.8 1.0 C B:ALA12 4.1 30.8 1.0 CA B:SER15 4.1 35.6 1.0 C4B B:FAD501 4.2 38.0 1.0 N B:ILE14 4.3 28.7 1.0 O3P B:FAD501 4.3 35.8 1.0 CA B:ALA12 4.4 25.2 1.0 CA B:ALA240 4.5 31.3 1.0 O2P B:FAD501 4.5 37.4 1.0 PA B:FAD501 4.7 31.7 1.0 OG B:SER15 4.7 37.1 1.0 O4B B:FAD501 4.7 38.2 1.0 C B:ILE14 4.8 31.5 1.0 O B:HOH638 4.9 47.4 1.0 C B:GLY16 4.9 33.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 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 L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg504 b:43.4 occ:1.00 O A:ALA240 2.7 28.5 1.0 N A:GLY16 3.0 32.4 1.0 O1P A:FAD501 3.1 29.8 1.0 N A:GLY13 3.2 30.9 1.0 CB A:ALA240 3.5 26.9 1.0 CA A:GLY13 3.5 26.2 1.0 C A:GLY11 3.6 34.4 1.0 O A:GLY11 3.7 30.9 1.0 CA A:GLY16 3.7 22.3 1.0 C A:ALA240 3.7 36.4 1.0 C A:GLY13 3.8 32.2 1.0 O5B A:FAD501 3.9 33.6 1.0 CB A:SER15 3.9 33.0 1.0 C5B A:FAD501 3.9 32.7 1.0 CA A:GLY11 4.0 27.1 1.0 N A:ALA12 4.0 33.8 1.0 N A:SER15 4.0 30.5 1.0 O A:GLY13 4.0 33.7 1.0 C A:SER15 4.0 36.6 1.0 C4B A:FAD501 4.1 33.5 1.0 CA A:SER15 4.1 31.4 1.0 P A:FAD501 4.2 32.0 1.0 CA A:ALA240 4.2 29.4 1.0 C A:ALA12 4.2 30.0 1.0 O3P A:FAD501 4.4 29.0 1.0 CA A:ALA12 4.5 28.4 1.0 O A:HOH655 4.5 37.2 1.0 N A:ILE14 4.6 30.2 1.0 O4B A:FAD501 4.6 33.5 1.0 O2P A:FAD501 4.6 33.7 1.0 OG A:SER15 4.8 31.8 1.0 N A:ILE241 4.8 34.6 1.0 PA A:FAD501 4.8 31.5 1.0 C A:GLY16 4.9 31.0 1.0 C A:ILE14 5.0 29.8 1.0

H.E.Lai, S.M.Chee, M.Morgan, S.J.Moore, K.M.Polizzi, P.S.Freemont. A Semi-Synthetic Strategy For Derivatization of the Violacein Natural Product Scaffold Biorxiv 2018.
DOI: 10.1101/202523