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Magnesium in PDB 6r4j: Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac

Enzymatic activity of Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac

All present enzymatic activity of Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac:
2.6.1.16;

Protein crystallography data

The structure of Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac, PDB code: 6r4j was solved by S.Ruegenberg, M.Horn, C.Pichlo, K.Allmeroth, U.Baumann, M.S.Denzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.73 / 2.42
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 153.227, 153.227, 162.544, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac (pdb code 6r4j). 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 Human Gfat-1 G451E in Complex with Udp-Glcnac, PDB code: 6r4j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6r4j

Go back to Magnesium Binding Sites List in 6r4j
Magnesium binding site 1 out of 2 in the Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac


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 Human Gfat-1 G451E in Complex with Udp-Glcnac within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg702

b:31.6
occ:1.00
O A:SER455 2.5 46.0 1.0
O2 A:UD1701 2.5 42.1 1.0
O A:THR458 2.6 43.1 1.0
O A:ARG456 2.8 49.6 1.0
HA A:ARG456 3.3 50.0 1.0
C2 A:UD1701 3.4 42.5 1.0
C A:ARG456 3.4 44.4 1.0
H1B A:UD1701 3.6 57.5 1.0
C A:SER455 3.6 44.7 1.0
C A:THR458 3.7 41.0 1.0
CA A:ARG456 3.8 41.6 1.0
HG1 A:THR458 3.9 45.4 1.0
OG1 A:THR458 4.0 37.8 1.0
O A:HOH875 4.0 47.9 1.0
H A:THR458 4.0 48.6 1.0
HN3 A:UD1701 4.1 54.5 1.0
N A:ARG456 4.2 40.1 1.0
N A:THR458 4.2 40.5 1.0
N3 A:UD1701 4.2 45.4 1.0
HA A:CYS460 4.3 43.2 1.0
N1 A:UD1701 4.3 49.2 1.0
C1B A:UD1701 4.4 47.9 1.0
N A:GLU457 4.4 40.3 1.0
C A:ASP459 4.4 40.6 1.0
CA A:THR458 4.4 41.3 1.0
O A:ASP459 4.5 42.2 1.0
N A:CYS460 4.6 41.6 1.0
HA A:ASP459 4.7 46.5 1.0
N A:ASP459 4.7 39.7 1.0
C A:GLU457 4.8 43.0 1.0
HA A:SER455 4.8 55.1 1.0
CB A:THR458 4.8 36.2 1.0
CA A:CYS460 4.9 36.0 1.0
CA A:SER455 4.9 45.9 1.0
CA A:ASP459 4.9 38.8 1.0
H A:GLU457 4.9 48.4 1.0
H A:CYS460 4.9 49.9 1.0
O4B A:UD1701 5.0 51.7 1.0

Magnesium binding site 2 out of 2 in 6r4j

Go back to Magnesium Binding Sites List in 6r4j
Magnesium binding site 2 out of 2 in the Crystal Structure of Human Gfat-1 G451E in Complex with Udp-Glcnac


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 Human Gfat-1 G451E in Complex with Udp-Glcnac within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg702

b:40.4
occ:1.00
O B:THR458 2.5 53.0 1.0
O B:SER455 2.6 61.9 1.0
O2 B:UD1701 2.6 62.5 1.0
O B:ARG456 2.6 53.4 1.0
HA B:ARG456 3.2 67.3 1.0
C B:ARG456 3.3 54.0 1.0
C2 B:UD1701 3.5 59.9 1.0
C B:THR458 3.7 48.7 1.0
C B:SER455 3.7 61.2 1.0
CA B:ARG456 3.7 56.0 1.0
H1B B:UD1701 3.8 72.3 1.0
H B:THR458 4.0 59.6 1.0
HG1 B:THR458 4.0 55.6 1.0
OG1 B:THR458 4.0 46.3 1.0
HN3 B:UD1701 4.1 70.0 1.0
N B:THR458 4.1 49.7 1.0
N B:ARG456 4.2 54.5 1.0
N3 B:UD1701 4.2 58.3 1.0
N B:GLU457 4.4 58.1 1.0
N1 B:UD1701 4.4 59.2 1.0
CA B:THR458 4.4 48.4 1.0
HA B:CYS460 4.4 64.0 1.0
O B:ASP459 4.4 56.3 1.0
C B:ASP459 4.5 53.5 1.0
C1B B:UD1701 4.5 60.2 1.0
HA B:ASP459 4.6 64.6 1.0
C B:GLU457 4.7 56.9 1.0
N B:ASP459 4.7 52.9 1.0
N B:CYS460 4.7 52.3 1.0
CB B:THR458 4.8 47.9 1.0
HA B:SER455 4.8 76.7 1.0
CA B:ASP459 4.9 53.8 1.0
CA B:SER455 4.9 63.9 1.0
H B:GLU457 4.9 69.7 1.0
CA B:GLU457 4.9 57.6 1.0

Reference:

S.Ruegenberg, M.Horn, C.Pichlo, K.Allmeroth, U.Baumann, M.S.Denzel. Loss of Gfat-1 Feedback Regulation Activates the Hexosamine Pathway That Modulates Protein Homeostasis To Be Published.
Page generated: Tue Oct 1 16:34:09 2024

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