Magnesium in PDB 5zlp: Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
Enzymatic activity of Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
All present enzymatic activity of Crystal Structure of Glutamine Synthetase From Helicobacter Pylori:
6.3.1.2;
Protein crystallography data
The structure of Crystal Structure of Glutamine Synthetase From Helicobacter Pylori, PDB code: 5zlp
was solved by
H.K.Joo,
J.Y.Lee,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.26 /
2.93
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
234.409,
135.167,
203.080,
90.00,
91.61,
90.00
|
R / Rfree (%)
|
16.8 /
24.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
(pdb code 5zlp). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Crystal Structure of Glutamine Synthetase From Helicobacter Pylori, PDB code: 5zlp:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 5zlp
Go back to
Magnesium Binding Sites List in 5zlp
Magnesium binding site 1 out
of 4 in the Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
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 Glutamine Synthetase From Helicobacter Pylori within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Mg503
b:41.9
occ:1.00
|
OE2
|
J:GLU230
|
2.0
|
36.3
|
1.0
|
OE2
|
J:GLU141
|
2.5
|
26.8
|
1.0
|
OE2
|
J:GLU223
|
2.5
|
30.8
|
1.0
|
OEA
|
J:PPQ502
|
2.6
|
36.0
|
0.8
|
CD
|
J:GLU230
|
2.9
|
37.6
|
1.0
|
OE1
|
J:GLU230
|
3.2
|
45.3
|
1.0
|
CD
|
J:GLU223
|
3.3
|
29.8
|
1.0
|
PDP
|
J:PPQ502
|
3.6
|
45.5
|
0.8
|
CD
|
J:GLU141
|
3.7
|
28.3
|
1.0
|
CEP
|
J:PPQ502
|
3.9
|
28.7
|
0.8
|
OE1
|
J:GLU223
|
3.9
|
33.4
|
1.0
|
OE2
|
J:GLU139
|
3.9
|
35.0
|
1.0
|
CE1
|
J:HIS279
|
4.0
|
27.0
|
1.0
|
ND1
|
J:HIS279
|
4.2
|
20.6
|
1.0
|
NE2
|
J:HIS221
|
4.2
|
22.9
|
1.0
|
CG
|
J:GLU223
|
4.2
|
19.6
|
1.0
|
CGP
|
J:PPQ502
|
4.3
|
35.4
|
0.8
|
CG
|
J:GLU230
|
4.3
|
21.2
|
1.0
|
CBP
|
J:PPQ502
|
4.4
|
31.1
|
0.8
|
CD
|
J:GLU139
|
4.4
|
42.1
|
1.0
|
CG
|
J:GLU141
|
4.4
|
23.2
|
1.0
|
CE1
|
J:HIS221
|
4.5
|
24.4
|
1.0
|
OE1
|
J:GLU141
|
4.5
|
29.6
|
1.0
|
OE1
|
J:GLU139
|
4.5
|
51.8
|
1.0
|
O
|
J:HOH601
|
4.6
|
39.6
|
1.0
|
CB
|
J:GLU230
|
4.8
|
17.9
|
1.0
|
OEB
|
J:PPQ502
|
4.9
|
37.2
|
0.8
|
|
Magnesium binding site 2 out
of 4 in 5zlp
Go back to
Magnesium Binding Sites List in 5zlp
Magnesium binding site 2 out
of 4 in the Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
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 Glutamine Synthetase From Helicobacter Pylori within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg502
b:48.4
occ:1.00
|
OE1
|
L:GLU230
|
2.4
|
40.0
|
1.0
|
OE2
|
L:GLU223
|
2.5
|
31.6
|
1.0
|
OE1
|
L:GLU141
|
2.5
|
30.9
|
1.0
|
OEB
|
L:P3P501
|
2.7
|
45.9
|
1.0
|
O15
|
L:P3P501
|
2.7
|
58.6
|
1.0
|
CD
|
L:GLU230
|
3.0
|
48.8
|
1.0
|
OE2
|
L:GLU230
|
3.0
|
57.1
|
1.0
|
P12
|
L:P3P501
|
3.2
|
78.6
|
1.0
|
CD
|
L:GLU223
|
3.4
|
31.9
|
1.0
|
CD
|
L:GLU141
|
3.4
|
25.9
|
1.0
|
O14
|
L:P3P501
|
3.7
|
47.9
|
1.0
|
OE1
|
L:GLU139
|
3.7
|
43.0
|
1.0
|
PDP
|
L:P3P501
|
3.8
|
51.8
|
1.0
|
CGP
|
L:P3P501
|
3.9
|
41.5
|
1.0
|
OE1
|
L:GLU223
|
3.9
|
39.2
|
1.0
|
ND1
|
L:HIS279
|
4.0
|
30.5
|
1.0
|
CG
|
L:GLU141
|
4.0
|
27.2
|
1.0
|
CE1
|
L:HIS279
|
4.0
|
36.4
|
1.0
|
CG
|
L:GLU230
|
4.3
|
29.4
|
1.0
|
OE2
|
L:GLU141
|
4.3
|
26.5
|
1.0
|
CE1
|
L:HIS221
|
4.4
|
27.2
|
1.0
|
MG
|
L:MG504
|
4.4
|
53.7
|
1.0
|
CG
|
L:GLU223
|
4.4
|
26.5
|
1.0
|
CEP
|
L:P3P501
|
4.5
|
43.2
|
1.0
|
O13
|
L:P3P501
|
4.6
|
68.5
|
1.0
|
CB
|
L:GLU230
|
4.6
|
24.5
|
1.0
|
NE2
|
L:HIS221
|
4.9
|
24.6
|
1.0
|
CBP
|
L:P3P501
|
4.9
|
34.9
|
1.0
|
CD
|
L:GLU139
|
5.0
|
41.3
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 5zlp
Go back to
Magnesium Binding Sites List in 5zlp
Magnesium binding site 3 out
of 4 in the Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of Glutamine Synthetase From Helicobacter Pylori within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg504
b:53.7
occ:1.00
|
OE2
|
L:GLU230
|
2.5
|
57.1
|
1.0
|
O2B
|
L:ADP503
|
3.0
|
80.2
|
1.0
|
O15
|
L:P3P501
|
3.0
|
58.6
|
1.0
|
NE2
|
L:HIS221
|
3.2
|
24.6
|
1.0
|
O2A
|
L:ADP503
|
3.7
|
70.8
|
1.0
|
CD
|
L:GLU230
|
3.8
|
48.8
|
1.0
|
CE1
|
L:HIS221
|
4.0
|
27.2
|
1.0
|
CG1
|
L:VAL219
|
4.1
|
25.1
|
1.0
|
CD2
|
L:HIS221
|
4.2
|
26.7
|
1.0
|
PB
|
L:ADP503
|
4.2
|
85.1
|
1.0
|
OE1
|
L:GLU139
|
4.2
|
43.0
|
1.0
|
O1B
|
L:ADP503
|
4.3
|
77.9
|
1.0
|
MG
|
L:MG502
|
4.4
|
48.4
|
1.0
|
P12
|
L:P3P501
|
4.4
|
78.6
|
1.0
|
CD
|
L:GLU139
|
4.6
|
41.3
|
1.0
|
OE1
|
L:GLU230
|
4.6
|
40.0
|
1.0
|
CG
|
L:GLU230
|
4.6
|
29.4
|
1.0
|
OE2
|
L:GLU139
|
4.7
|
47.4
|
1.0
|
O14
|
L:P3P501
|
4.9
|
47.9
|
1.0
|
O3A
|
L:ADP503
|
5.0
|
61.8
|
1.0
|
PA
|
L:ADP503
|
5.0
|
70.8
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 5zlp
Go back to
Magnesium Binding Sites List in 5zlp
Magnesium binding site 4 out
of 4 in the Crystal Structure of Glutamine Synthetase From Helicobacter Pylori
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of Glutamine Synthetase From Helicobacter Pylori within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mg503
b:44.2
occ:1.00
|
OE2
|
I:GLU230
|
1.6
|
48.1
|
1.0
|
OEA
|
I:PPQ502
|
1.8
|
51.2
|
1.0
|
OE2
|
I:GLU223
|
2.5
|
27.9
|
1.0
|
CD
|
I:GLU230
|
2.6
|
50.0
|
1.0
|
OE2
|
I:GLU141
|
2.8
|
24.4
|
1.0
|
OE1
|
I:GLU230
|
3.0
|
50.8
|
1.0
|
PDP
|
I:PPQ502
|
3.2
|
58.6
|
1.0
|
CD
|
I:GLU223
|
3.4
|
31.8
|
1.0
|
OE1
|
I:GLU139
|
3.8
|
39.1
|
1.0
|
CD
|
I:GLU141
|
3.8
|
28.2
|
1.0
|
CG
|
I:GLU230
|
3.8
|
28.8
|
1.0
|
OEB
|
I:PPQ502
|
3.9
|
47.6
|
1.0
|
CEP
|
I:PPQ502
|
4.0
|
40.6
|
1.0
|
CG
|
I:GLU141
|
4.0
|
28.9
|
1.0
|
OE1
|
I:GLU223
|
4.1
|
34.2
|
1.0
|
NE2
|
I:HIS221
|
4.3
|
25.6
|
1.0
|
CE1
|
I:HIS221
|
4.3
|
27.7
|
1.0
|
CG
|
I:GLU223
|
4.4
|
27.8
|
1.0
|
CB
|
I:GLU230
|
4.4
|
24.2
|
1.0
|
CE1
|
I:HIS279
|
4.5
|
26.5
|
1.0
|
CBP
|
I:PPQ502
|
4.5
|
36.4
|
1.0
|
ND1
|
I:HIS279
|
4.5
|
22.1
|
1.0
|
CGP
|
I:PPQ502
|
4.5
|
35.1
|
1.0
|
CD
|
I:GLU139
|
4.7
|
47.1
|
1.0
|
OE1
|
I:GLU141
|
5.0
|
22.3
|
1.0
|
|
Reference:
H.K.Joo,
Y.W.Park,
Y.Y.Jang,
J.Y.Lee.
Structural Analysis of Glutamine Synthetase From Helicobacter Pylori. Sci Rep V. 8 11657 2018.
ISSN: ESSN 2045-2322
PubMed: 30076387
DOI: 10.1038/S41598-018-30191-5
Page generated: Mon Sep 30 18:40:33 2024
|