Magnesium in PDB 6ayu: Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis
Enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis
All present enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis:
3.1.3.11;
Protein crystallography data
The structure of Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis, PDB code: 6ayu
was solved by
C.Abad-Zapatero,
N.Wolf,
H.J.Gutka,
F.Movahedzadeh,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.50 /
2.20
|
Space group
|
P 61 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
130.890,
130.890,
142.848,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
20.4 /
25.2
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis
(pdb code 6ayu). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the
Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis, PDB code: 6ayu:
Jump to Magnesium binding site number:
1;
2;
3;
Magnesium binding site 1 out
of 3 in 6ayu
Go back to
Magnesium Binding Sites List in 6ayu
Magnesium binding site 1 out
of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis
 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 Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg402
b:57.0
occ:1.00
|
OD2
|
A:ASP79
|
2.4
|
60.1
|
1.0
|
OE2
|
A:GLU208
|
2.7
|
49.1
|
1.0
|
OD1
|
A:ASP82
|
2.8
|
42.9
|
1.0
|
O2
|
A:GOL407
|
3.0
|
80.1
|
1.0
|
CG
|
A:ASP79
|
3.2
|
51.4
|
1.0
|
OD1
|
A:ASP79
|
3.3
|
51.7
|
1.0
|
O1
|
A:F6P401
|
3.3
|
67.0
|
1.0
|
CG
|
A:GLU208
|
3.4
|
39.3
|
1.0
|
CA
|
A:ASP82
|
3.4
|
48.2
|
1.0
|
CD
|
A:GLU208
|
3.5
|
47.8
|
1.0
|
N
|
A:GLY83
|
3.7
|
57.0
|
1.0
|
CG
|
A:ASP82
|
3.7
|
48.7
|
1.0
|
C1
|
A:F6P401
|
3.7
|
59.6
|
1.0
|
C
|
A:ASP82
|
3.9
|
52.6
|
1.0
|
O
|
A:ILE81
|
3.9
|
46.8
|
1.0
|
CB
|
A:ASP82
|
3.9
|
46.1
|
1.0
|
C3
|
A:F6P401
|
4.0
|
49.2
|
1.0
|
C2
|
A:GOL407
|
4.1
|
84.1
|
1.0
|
O3
|
A:F6P401
|
4.2
|
45.3
|
1.0
|
O
|
A:HOH530
|
4.3
|
67.3
|
1.0
|
O
|
A:HOH554
|
4.4
|
61.2
|
1.0
|
O
|
A:HOH567
|
4.4
|
64.0
|
1.0
|
N
|
A:ASP82
|
4.4
|
43.0
|
1.0
|
C2
|
A:F6P401
|
4.5
|
61.3
|
1.0
|
O1
|
A:GOL407
|
4.5
|
71.5
|
1.0
|
C
|
A:ILE81
|
4.6
|
45.9
|
1.0
|
CB
|
A:ASP79
|
4.6
|
44.8
|
1.0
|
OE1
|
A:GLU208
|
4.7
|
46.6
|
1.0
|
C1
|
A:GOL407
|
4.8
|
82.8
|
1.0
|
CA
|
A:GLY83
|
4.9
|
58.1
|
1.0
|
O
|
A:ASP82
|
4.9
|
50.3
|
1.0
|
OD2
|
A:ASP82
|
4.9
|
51.2
|
1.0
|
CB
|
A:GLU208
|
4.9
|
40.7
|
1.0
|
|
Magnesium binding site 2 out
of 3 in 6ayu
Go back to
Magnesium Binding Sites List in 6ayu
Magnesium binding site 2 out
of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis
 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 Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg406
b:57.2
occ:1.00
|
O
|
A:ARG192
|
2.3
|
64.3
|
1.0
|
O
|
A:THR197
|
2.4
|
50.0
|
1.0
|
OG
|
A:SER195
|
2.8
|
60.9
|
1.0
|
O
|
A:ALA190
|
2.8
|
53.6
|
1.0
|
O
|
A:SER189
|
2.9
|
54.9
|
1.0
|
C
|
A:ALA190
|
3.5
|
51.5
|
1.0
|
C
|
A:ARG192
|
3.5
|
61.4
|
1.0
|
C
|
A:THR197
|
3.6
|
54.3
|
1.0
|
O
|
A:PRO193
|
3.8
|
91.0
|
1.0
|
CB
|
A:SER195
|
3.9
|
60.1
|
1.0
|
CA
|
A:ALA190
|
4.0
|
48.9
|
1.0
|
N
|
A:SER195
|
4.0
|
65.0
|
1.0
|
C
|
A:SER189
|
4.0
|
54.9
|
1.0
|
C
|
A:PRO193
|
4.1
|
80.8
|
1.0
|
N
|
A:ARG192
|
4.1
|
54.2
|
1.0
|
O
|
A:HOH508
|
4.3
|
50.4
|
1.0
|
CA
|
A:ARG192
|
4.3
|
59.9
|
1.0
|
N
|
A:THR197
|
4.3
|
56.0
|
1.0
|
CA
|
A:ASP198
|
4.4
|
49.8
|
1.0
|
OG1
|
A:THR197
|
4.4
|
65.3
|
1.0
|
C
|
A:CYS191
|
4.4
|
57.6
|
1.0
|
N
|
A:CYS191
|
4.4
|
49.5
|
1.0
|
N
|
A:ASP198
|
4.4
|
55.7
|
1.0
|
N
|
A:PRO193
|
4.5
|
68.2
|
1.0
|
CA
|
A:SER195
|
4.5
|
56.5
|
1.0
|
N
|
A:ALA190
|
4.5
|
50.4
|
1.0
|
CA
|
A:PRO193
|
4.5
|
72.0
|
1.0
|
CA
|
A:THR197
|
4.5
|
59.6
|
1.0
|
N
|
A:HIS194
|
4.6
|
74.7
|
1.0
|
N
|
A:GLY196
|
4.7
|
55.0
|
1.0
|
CB
|
A:ARG192
|
4.8
|
56.1
|
1.0
|
CA
|
A:CYS191
|
4.8
|
51.0
|
1.0
|
O
|
A:CYS191
|
4.9
|
56.5
|
1.0
|
C
|
A:SER195
|
4.9
|
58.9
|
1.0
|
OD1
|
A:ASP198
|
4.9
|
57.7
|
1.0
|
|
Magnesium binding site 3 out
of 3 in 6ayu
Go back to
Magnesium Binding Sites List in 6ayu
Magnesium binding site 3 out
of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis
 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 Fructose-1,6-Bisphosphatase T84S From Mycobacterium Tuberculosis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg403
b:63.2
occ:1.00
|
OD2
|
B:ASP79
|
2.3
|
56.6
|
1.0
|
OD1
|
B:ASP82
|
2.4
|
53.0
|
1.0
|
OE2
|
B:GLU208
|
2.8
|
56.5
|
1.0
|
CG
|
B:ASP79
|
3.2
|
59.9
|
1.0
|
CG
|
B:ASP82
|
3.3
|
52.6
|
1.0
|
O
|
B:HOH510
|
3.4
|
60.5
|
1.0
|
C1
|
B:F6P401
|
3.4
|
59.0
|
1.0
|
CG
|
B:GLU208
|
3.4
|
50.9
|
1.0
|
CA
|
B:ASP82
|
3.4
|
55.7
|
1.0
|
OD1
|
B:ASP79
|
3.5
|
58.0
|
1.0
|
CD
|
B:GLU208
|
3.5
|
54.6
|
1.0
|
CB
|
B:ASP82
|
3.8
|
51.9
|
1.0
|
C3
|
B:F6P401
|
3.8
|
62.9
|
1.0
|
O3
|
B:F6P401
|
3.9
|
57.1
|
1.0
|
N
|
B:GLY83
|
4.0
|
57.7
|
1.0
|
C
|
B:ASP82
|
4.0
|
60.4
|
1.0
|
O1
|
B:F6P401
|
4.1
|
75.3
|
1.0
|
C2
|
B:F6P401
|
4.2
|
64.0
|
1.0
|
O
|
B:ILE81
|
4.3
|
52.9
|
1.0
|
O
|
B:HOH578
|
4.4
|
69.8
|
1.0
|
OD2
|
B:ASP82
|
4.4
|
52.3
|
1.0
|
N
|
B:ASP82
|
4.5
|
53.0
|
1.0
|
CB
|
B:ASP79
|
4.6
|
51.7
|
1.0
|
OE1
|
B:GLU208
|
4.8
|
46.5
|
1.0
|
C
|
B:ILE81
|
4.8
|
51.7
|
1.0
|
CB
|
B:GLU208
|
4.9
|
46.2
|
1.0
|
O
|
B:ASP82
|
4.9
|
54.3
|
1.0
|
|
Reference:
N.M.Wolf,
H.J.Gutka,
F.Movahedzadeh,
C.Abad-Zapatero.
Structures of the Mycobacterium Tuberculosis Glpx Protein (Class II Fructose-1,6-Bisphosphatase): Implications For the Active Oligomeric State, Catalytic Mechanism and Citrate Inhibition. Acta Crystallogr D Struct V. 74 321 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 29652259
DOI: 10.1107/S2059798318002838
Page generated: Mon Sep 30 19:24:56 2024
|