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Magnesium in PDB 6fw9: Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-L-Tryptophan

Enzymatic activity of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-L-Tryptophan

All present enzymatic activity of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-L-Tryptophan:
1.4.3.23;

Protein crystallography data

The structure of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-L-Tryptophan, PDB code: 6fw9 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) 63.86 / 2.74
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 151.478, 174.322, 93.821, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 26.1

Other elements in 6fw9:

The structure of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-L-Tryptophan also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-L-Tryptophan (pdb code 6fw9). 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 6-Fluoro-L-Tryptophan, PDB code: 6fw9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6fw9

Go back to Magnesium Binding Sites List in 6fw9
Magnesium binding site 1 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-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 6-Fluoro-L-Tryptophan within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:50.8
occ:1.00
 O1P B:FAD501 2.5 42.0 1.0
N B:GLY13 2.8 35.6 1.0
CA B:GLY13 2.9 37.8 1.0
N B:GLY16 3.1 45.1 1.0
C B:GLY13 3.2 41.4 1.0
O B:ALA240 3.2 49.4 1.0
O B:GLY13 3.5 40.6 1.0
CB B:SER15 3.6 40.4 1.0
O5B B:FAD501 3.6 35.3 1.0
P B:FAD501 3.6 40.1 1.0
N B:SER15 3.6 35.8 1.0
O3P B:FAD501 3.7 45.5 1.0
N B:ILE14 3.8 41.6 1.0
C5B B:FAD501 3.9 36.8 1.0
CA B:SER15 3.9 35.2 1.0
CA B:GLY16 4.0 45.1 1.0
C B:SER15 4.0 45.4 1.0
C B:ALA12 4.0 40.8 1.0
C4B B:FAD501 4.0 41.2 1.0
CB B:ALA240 4.1 47.5 1.0
N B:ALA12 4.1 39.4 1.0
OG B:SER15 4.1 51.6 1.0
O2P B:FAD501 4.1 51.4 1.0
C B:GLY11 4.2 39.7 1.0
C B:ALA240 4.2 53.8 1.0
PA B:FAD501 4.3 38.0 1.0
O B:GLY11 4.4 43.4 1.0
CA B:ALA12 4.5 33.2 1.0
C B:ILE14 4.5 37.9 1.0
CA B:GLY11 4.5 40.9 1.0
CA B:ALA240 4.8 45.9 1.0
O4B B:FAD501 4.8 42.8 1.0
CA B:ILE14 4.8 32.6 1.0
O5' B:FAD501 4.9 41.9 1.0
O2A B:FAD501 4.9 38.6 1.0
N B:LEU17 4.9 39.5 1.0
O B:HOH607 5.0 40.4 1.0
O B:ALA12 5.0 46.5 1.0

Magnesium binding site 2 out of 2 in 6fw9

Go back to Magnesium Binding Sites List in 6fw9
Magnesium binding site 2 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum in Complex with 6-Fluoro-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 6-Fluoro-L-Tryptophan within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:59.5
occ:1.00
 O A:ALA240 2.7 48.5 1.0
N A:GLY16 2.8 42.7 1.0
O1P A:FAD501 2.9 35.4 1.0
N A:GLY13 3.0 36.8 1.0
CA A:GLY13 3.4 43.0 1.0
CB A:ALA240 3.4 43.9 1.0
CA A:GLY16 3.5 36.2 1.0
C A:GLY11 3.6 42.5 1.0
CB A:SER15 3.7 35.2 1.0
C A:GLY13 3.7 45.6 1.0
O A:GLY11 3.7 48.5 1.0
C A:ALA240 3.7 48.2 1.0
O5B A:FAD501 3.7 42.3 1.0
C A:SER15 3.8 49.6 1.0
N A:SER15 3.9 34.8 1.0
O A:GLY13 3.9 41.8 1.0
N A:ALA12 3.9 36.5 1.0
CA A:SER15 4.0 34.6 1.0
CA A:GLY11 4.0 43.6 1.0
C A:ALA12 4.1 41.3 1.0
P A:FAD501 4.2 42.2 1.0
CA A:ALA240 4.2 42.0 1.0
C5B A:FAD501 4.3 46.9 1.0
N A:ILE14 4.3 41.2 1.0
CA A:ALA12 4.3 37.6 1.0
C4B A:FAD501 4.3 43.5 1.0
OG A:SER15 4.6 49.5 1.0
O2P A:FAD501 4.6 42.0 1.0
C A:ILE14 4.7 41.7 1.0
O4B A:FAD501 4.7 41.5 1.0
C A:GLY16 4.7 39.7 1.0
O3P A:FAD501 4.8 45.4 1.0
N A:ILE241 4.9 41.2 1.0
N A:LEU17 4.9 37.3 1.0
PA A:FAD501 4.9 37.8 1.0
O A:SER15 4.9 54.4 1.0
O A:HOH622 5.0 49.9 1.0

Reference:

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
Page generated: Tue Oct 1 00:53:26 2024

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