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Magnesium in PDB 3c4q: Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp

Protein crystallography data

The structure of Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp, PDB code: 3c4q was solved by M.W.Vetting, P.A.Frantom, J.S.Blanchard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 78.25 / 2.80
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 224.245, 224.245, 125.112, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp (pdb code 3c4q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp, PDB code: 3c4q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3c4q

Go back to Magnesium Binding Sites List in 3c4q
Magnesium binding site 1 out of 2 in the Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:42.3
occ:1.00
OG1 A:THR330 2.2 27.4 1.0
O A:ALA306 2.3 25.1 1.0
O A:HOH606 2.4 17.1 1.0
O A:ARG304 2.7 23.1 1.0
O A:TYR303 2.7 23.8 1.0
C A:ARG304 3.3 22.2 1.0
CB A:THR330 3.4 27.1 1.0
C A:ALA306 3.4 24.6 1.0
CG2 A:THR330 3.6 26.8 1.0
CA A:ARG304 3.7 21.3 1.0
C A:TYR303 3.8 22.5 1.0
N A:ALA306 3.9 22.7 1.0
CA A:THR330 4.1 27.0 1.0
CA A:ALA306 4.2 23.8 1.0
N A:ARG304 4.2 22.1 1.0
N A:ALA305 4.4 22.5 1.0
C A:ALA305 4.4 22.5 1.0
N A:ASP307 4.5 24.6 1.0
N A:THR330 4.6 26.9 1.0
OG1 A:THR210 4.6 35.9 1.0
O A:SER328 4.6 27.3 1.0
CB A:ALA306 4.7 22.8 1.0
O A:GLY329 4.7 27.4 1.0
CA A:ASP307 4.7 25.0 1.0
C A:GLY329 4.8 27.1 1.0
CA A:ALA305 4.9 22.6 1.0
O A:ALA305 4.9 22.0 1.0
CB A:ARG304 5.0 20.9 1.0

Magnesium binding site 2 out of 2 in 3c4q

Go back to Magnesium Binding Sites List in 3c4q
Magnesium binding site 2 out of 2 in the Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Retaining Glycosyltransferase Msha : the First Step in Mycothiol Biosynthesis. Organism : Corynebacterium Glutamicum- Complex with Udp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:32.5
occ:1.00
O B:HOH606 2.2 28.0 1.0
O B:ALA306 2.4 22.0 1.0
O B:HOH624 2.6 19.1 1.0
OG1 B:THR330 2.7 26.9 1.0
O B:TYR303 2.8 20.4 1.0
O B:ARG304 2.9 19.9 1.0
C B:ARG304 3.3 19.0 1.0
C B:ALA306 3.5 22.1 1.0
CA B:ARG304 3.6 18.2 1.0
CB B:THR330 3.8 27.6 1.0
C B:TYR303 3.9 20.1 1.0
CG2 B:THR330 3.9 28.3 1.0
N B:ALA306 3.9 19.9 1.0
OG1 B:THR210 4.2 29.7 1.0
N B:ALA305 4.2 19.9 1.0
C B:ALA305 4.2 19.4 1.0
N B:ARG304 4.2 18.9 1.0
CA B:ALA306 4.2 21.4 1.0
CA B:THR330 4.4 27.9 1.0
O B:GLY329 4.5 29.3 1.0
N B:ASP307 4.6 23.1 1.0
O B:ALA305 4.7 18.3 1.0
CA B:ALA305 4.7 19.6 1.0
N B:THR330 4.7 28.3 1.0
C B:GLY329 4.8 28.8 1.0
CA B:ASP307 4.8 24.9 1.0
CB B:ALA306 4.8 21.2 1.0
O B:HOH625 4.8 17.6 1.0
CB B:ARG304 4.9 18.0 1.0
CG2 B:THR210 4.9 30.1 1.0
O B:SER328 5.0 31.3 1.0

Reference:

M.W.Vetting, P.A.Frantom, J.S.Blanchard. Structural and Enzymatic Analysis of Msha From Corynebacterium Glutamicum: Substrate-Assisted Catalysis J.Biol.Chem. V. 283 15834 2008.
ISSN: ISSN 0021-9258
PubMed: 18390549
DOI: 10.1074/JBC.M801017200
Page generated: Wed Aug 14 09:25:39 2024

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