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Magnesium in PDB 8enk: Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp

Enzymatic activity of Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp

All present enzymatic activity of Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp:
3.6.4.13;

Protein crystallography data

The structure of Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp, PDB code: 8enk was solved by Y.Xie, Y.Ren, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.72 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 88.534, 96.786, 126.18, 90, 90, 90
R / Rfree (%) 22.4 / 25.3

Other elements in 8enk:

The structure of Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp (pdb code 8enk). 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 UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp, PDB code: 8enk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8enk

Go back to Magnesium Binding Sites List in 8enk
Magnesium binding site 1 out of 2 in the Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp


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 UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:50.5
occ:1.00
O A:HOH1103 2.1 44.5 1.0
O A:HOH1108 2.1 49.9 1.0
F3 A:BEF1001 2.1 49.3 1.0
O A:HOH1101 2.1 50.6 1.0
O A:HOH1102 2.3 47.2 1.0
O2B A:ADP1000 2.3 47.5 1.0
OD2 A:ASP196 3.3 44.6 1.0
OG1 A:THR96 3.4 47.3 1.0
BE A:BEF1001 3.4 50.2 1.0
PB A:ADP1000 3.6 48.0 1.0
OE2 A:GLU197 3.8 44.3 1.0
OD1 A:ASP196 3.8 46.6 1.0
O1B A:ADP1000 3.8 51.4 1.0
CG A:ASP196 4.0 45.2 1.0
F2 A:BEF1001 4.1 51.3 1.0
O1A A:ADP1000 4.2 52.4 1.0
CA A:GLY350 4.5 45.0 1.0
F1 A:BEF1001 4.5 49.3 1.0
O3A A:ADP1000 4.6 50.9 1.0
O2A A:ADP1000 4.6 50.6 1.0
O3B A:ADP1000 4.6 53.2 1.0
PA A:ADP1000 4.6 49.9 1.0
O A:GLY350 4.7 43.2 1.0
CB A:THR96 4.7 47.2 1.0
N A:THR96 4.7 48.1 1.0
CE A:LYS95 4.8 52.2 1.0
CD A:GLU197 4.9 44.9 1.0
O A:HOH1107 4.9 50.0 1.0
CB A:LYS95 4.9 50.0 1.0

Magnesium binding site 2 out of 2 in 8enk

Go back to Magnesium Binding Sites List in 8enk
Magnesium binding site 2 out of 2 in the Crystal Structure of UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp


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 UAP56 in Complex with THO1, the Yeast Homolog of Human Sarnp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1002

b:54.9
occ:1.00
O B:HOH1106 2.0 56.2 1.0
O B:HOH1104 2.0 57.7 1.0
O B:HOH1103 2.1 50.9 1.0
F3 B:BEF1001 2.1 51.3 1.0
O B:HOH1101 2.3 50.6 1.0
O1B B:ADP1000 2.7 50.5 1.0
OD2 B:ASP196 3.1 53.2 1.0
BE B:BEF1001 3.5 53.8 1.0
OD1 B:ASP196 3.6 51.8 1.0
PB B:ADP1000 3.8 51.8 1.0
O2B B:ADP1000 3.8 52.9 1.0
CG B:ASP196 3.8 53.4 1.0
OE2 B:GLU197 3.8 57.5 1.0
CA B:GLY350 3.9 52.5 1.0
OG1 B:THR96 3.9 52.2 1.0
O B:GLY350 4.3 48.0 1.0
F2 B:BEF1001 4.4 53.6 1.0
O2A B:ADP1000 4.5 52.7 1.0
O B:HOH1109 4.5 55.9 1.0
F1 B:BEF1001 4.5 54.5 1.0
C B:GLY350 4.6 47.6 1.0
CD B:GLU197 4.7 56.6 1.0
O3A B:ADP1000 4.8 52.8 1.0
O B:HOH1102 4.9 52.5 1.0
N B:GLY350 4.9 51.7 1.0
CD1 B:LEU125 4.9 49.5 1.0
O3B B:ADP1000 4.9 53.4 1.0
PA B:ADP1000 4.9 50.7 1.0
O1A B:ADP1000 4.9 50.1 1.0
CG B:GLU197 5.0 55.4 1.0

Reference:

Y.Xie, Y.Ren. Structural Basis For High Order Complex of Sarnp and DDX39B to Facilitate Mrnp Assembly Cell Rep 2023.
ISSN: ESSN 2211-1247
Page generated: Thu Dec 28 09:00:41 2023

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