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Magnesium in PDB 4c7x: Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution

Enzymatic activity of Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution

All present enzymatic activity of Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution:
2.2.1.1;

Protein crystallography data

The structure of Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution, PDB code: 4c7x was solved by C.M.C.Lobley, P.Lukacik, M.Bumann, P.Aller, A.Douangamath, P.W.O'toole, M.A.Walsh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.69 / 2.29
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 74.990, 74.990, 192.850, 90.00, 90.00, 120.00
R / Rfree (%) 15.378 / 23.565

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution (pdb code 4c7x). 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 Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution, PDB code: 4c7x:

Magnesium binding site 1 out of 1 in 4c7x

Go back to Magnesium Binding Sites List in 4c7x
Magnesium binding site 1 out of 1 in the Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Thiamine Pyrophosphate Bound Tranksetolase From Lactobacillus Salivarius at 2.2A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg700

b:31.9
occ:1.00
 O A:ILE190 1.9 36.1 1.0
O1B A:TPP701 1.9 44.8 1.0
O2A A:TPP701 2.1 47.5 1.0
OD2 A:ASP158 2.2 29.3 1.0
OD1 A:ASN188 2.2 31.7 1.0
O A:HOH2070 2.2 26.9 1.0
CG A:ASN188 3.0 34.6 1.0
C A:ILE190 3.1 34.2 1.0
ND2 A:ASN188 3.2 40.6 1.0
CG A:ASP158 3.2 28.4 1.0
PA A:TPP701 3.3 40.7 1.0
PB A:TPP701 3.3 47.6 1.0
O3A A:TPP701 3.6 42.1 1.0
CB A:ASP158 3.7 27.0 1.0
N A:ILE190 3.8 30.6 1.0
CA A:ILE190 3.9 31.5 1.0
O3B A:TPP701 4.0 52.0 1.0
N A:SER191 4.1 35.0 1.0
N A:ASP158 4.1 26.2 1.0
O7 A:TPP701 4.3 42.9 1.0
O A:HOH2087 4.3 32.0 1.0
OD1 A:ASP158 4.3 27.1 1.0
CA A:SER191 4.3 33.7 1.0
O1A A:TPP701 4.4 39.9 1.0
CB A:ILE190 4.4 34.2 1.0
CB A:ASN188 4.4 32.8 1.0
O A:ASP186 4.5 32.9 1.0
O2B A:TPP701 4.5 54.0 1.0
CA A:ASP158 4.5 27.0 1.0
N A:ASN188 4.6 35.3 1.0
N A:GLY189 4.8 34.9 1.0
CA A:ASN188 4.9 33.9 1.0
C A:ASN188 4.9 34.2 1.0
CG2 A:ILE190 5.0 33.2 1.0
C A:GLY189 5.0 34.3 1.0

Reference:

C.M.C.Lobley, P.Lukacik, M.Bumann, P.Aller, A.Douangamath, P.W.O'toole, M.A.Walsh. High Resolution Crystal Structures of Lactobacillus Salivarius Transketolase in the Presence and Absence of Thiamine Pyrophosphate To Be Published.
Page generated: Mon Dec 14 09:16:34 2020

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