Magnesium in PDB 3wt0: Crystal Structure Analysis of Cell Division Protein
Protein crystallography data
The structure of Crystal Structure Analysis of Cell Division Protein, PDB code: 3wt0
was solved by
K.Kato,
T.Ishido,
T.Matsui,
M.Yao,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.54 /
2.00
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
106.032,
70.628,
120.676,
90.00,
108.00,
90.00
|
R / Rfree (%)
|
20.8 /
23.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure Analysis of Cell Division Protein
(pdb code 3wt0). 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 Analysis of Cell Division Protein, PDB code: 3wt0:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 3wt0
Go back to
Magnesium Binding Sites List in 3wt0
Magnesium binding site 1 out
of 4 in the Crystal Structure Analysis of Cell Division Protein
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure Analysis of Cell Division Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg401
b:35.0
occ:1.00
|
O1B
|
A:ATP400
|
2.0
|
38.8
|
1.0
|
O
|
A:HOH633
|
2.0
|
38.7
|
1.0
|
O
|
A:HOH603
|
2.0
|
35.0
|
1.0
|
O1G
|
A:ATP400
|
2.0
|
37.5
|
1.0
|
O
|
A:HOH601
|
2.1
|
32.1
|
1.0
|
O
|
A:HOH602
|
2.2
|
29.6
|
1.0
|
PB
|
A:ATP400
|
3.3
|
37.6
|
1.0
|
PG
|
A:ATP400
|
3.4
|
33.9
|
1.0
|
O3B
|
A:ATP400
|
3.7
|
34.4
|
1.0
|
O3A
|
A:ATP400
|
3.9
|
34.3
|
1.0
|
O
|
A:HOH514
|
3.9
|
47.6
|
1.0
|
O
|
A:HOH605
|
3.9
|
40.1
|
1.0
|
O2A
|
A:ATP400
|
4.0
|
34.3
|
1.0
|
O
|
A:HOH517
|
4.0
|
33.0
|
1.0
|
NZ
|
A:LYS77
|
4.1
|
34.2
|
1.0
|
O2G
|
A:ATP400
|
4.1
|
35.6
|
1.0
|
OD2
|
A:ASP10
|
4.2
|
39.9
|
1.0
|
OD1
|
A:ASP10
|
4.4
|
42.9
|
1.0
|
NZ
|
A:LYS17
|
4.5
|
41.4
|
1.0
|
OD2
|
A:ASP206
|
4.5
|
52.5
|
1.0
|
O3G
|
A:ATP400
|
4.5
|
32.2
|
1.0
|
PA
|
A:ATP400
|
4.5
|
35.2
|
1.0
|
O2B
|
A:ATP400
|
4.5
|
34.2
|
1.0
|
OD1
|
A:ASP206
|
4.6
|
46.7
|
1.0
|
O
|
A:HOH567
|
4.7
|
37.6
|
1.0
|
CG
|
A:ASP10
|
4.7
|
39.9
|
1.0
|
CA
|
A:GLY208
|
4.8
|
26.7
|
1.0
|
CG
|
A:ASP206
|
4.9
|
47.8
|
1.0
|
CA
|
A:GLY12
|
4.9
|
34.9
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 3wt0
Go back to
Magnesium Binding Sites List in 3wt0
Magnesium binding site 2 out
of 4 in the Crystal Structure Analysis of Cell Division Protein
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure Analysis of Cell Division Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg401
b:35.0
occ:1.00
|
O3G
|
B:ATP400
|
1.9
|
43.7
|
1.0
|
O1B
|
B:ATP400
|
1.9
|
35.2
|
1.0
|
O
|
B:HOH595
|
1.9
|
28.8
|
1.0
|
O
|
B:HOH638
|
2.0
|
29.8
|
1.0
|
O
|
B:HOH504
|
2.1
|
26.5
|
1.0
|
O
|
B:HOH503
|
2.2
|
26.2
|
1.0
|
PB
|
B:ATP400
|
3.2
|
24.8
|
1.0
|
PG
|
B:ATP400
|
3.2
|
32.2
|
1.0
|
O3B
|
B:ATP400
|
3.5
|
32.7
|
1.0
|
O3A
|
B:ATP400
|
3.8
|
30.1
|
1.0
|
O1G
|
B:ATP400
|
4.0
|
35.0
|
1.0
|
O
|
B:HOH517
|
4.0
|
23.5
|
1.0
|
O2A
|
B:ATP400
|
4.0
|
36.4
|
1.0
|
O
|
B:HOH505
|
4.0
|
27.0
|
1.0
|
O
|
B:HOH502
|
4.0
|
26.5
|
1.0
|
NZ
|
B:LYS77
|
4.1
|
25.3
|
1.0
|
OD2
|
B:ASP10
|
4.2
|
39.9
|
1.0
|
O2G
|
B:ATP400
|
4.3
|
40.6
|
1.0
|
O2B
|
B:ATP400
|
4.4
|
28.8
|
1.0
|
OD1
|
B:ASP10
|
4.4
|
35.8
|
1.0
|
PA
|
B:ATP400
|
4.5
|
28.1
|
1.0
|
O
|
B:HOH634
|
4.5
|
28.9
|
1.0
|
NZ
|
B:LYS17
|
4.6
|
35.9
|
1.0
|
OD1
|
B:ASP206
|
4.6
|
43.1
|
1.0
|
OD2
|
B:ASP206
|
4.6
|
39.5
|
1.0
|
CA
|
B:GLY208
|
4.8
|
27.2
|
1.0
|
CG
|
B:ASP10
|
4.8
|
36.4
|
1.0
|
CA
|
B:GLY12
|
4.9
|
22.7
|
1.0
|
CG
|
B:ASP206
|
4.9
|
40.2
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 3wt0
Go back to
Magnesium Binding Sites List in 3wt0
Magnesium binding site 3 out
of 4 in the Crystal Structure Analysis of Cell Division Protein
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure Analysis of Cell Division Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg401
b:35.8
occ:1.00
|
O1B
|
C:ATP400
|
1.9
|
26.0
|
1.0
|
O2G
|
C:ATP400
|
2.0
|
42.2
|
1.0
|
O
|
C:HOH711
|
2.0
|
30.5
|
1.0
|
O
|
C:HOH503
|
2.0
|
26.4
|
1.0
|
O
|
C:HOH527
|
2.1
|
28.9
|
1.0
|
O
|
C:HOH504
|
2.3
|
32.3
|
1.0
|
PB
|
C:ATP400
|
3.2
|
28.8
|
1.0
|
PG
|
C:ATP400
|
3.3
|
27.5
|
1.0
|
O3B
|
C:ATP400
|
3.6
|
33.7
|
1.0
|
O
|
C:HOH714
|
3.7
|
50.7
|
1.0
|
O
|
C:HOH528
|
3.7
|
37.0
|
1.0
|
O3A
|
C:ATP400
|
3.8
|
31.2
|
1.0
|
O
|
C:HOH613
|
3.8
|
47.2
|
1.0
|
OD2
|
C:ASP206
|
3.9
|
63.0
|
1.0
|
O
|
C:HOH532
|
3.9
|
28.6
|
1.0
|
O2A
|
C:ATP400
|
4.0
|
38.4
|
1.0
|
NZ
|
C:LYS77
|
4.0
|
28.2
|
1.0
|
O3G
|
C:ATP400
|
4.1
|
33.6
|
1.0
|
OD2
|
C:ASP10
|
4.3
|
42.7
|
1.0
|
OD1
|
C:ASP10
|
4.4
|
39.2
|
1.0
|
O1G
|
C:ATP400
|
4.4
|
35.2
|
1.0
|
O2B
|
C:ATP400
|
4.5
|
26.3
|
1.0
|
PA
|
C:ATP400
|
4.5
|
29.7
|
1.0
|
NZ
|
C:LYS17
|
4.5
|
42.9
|
1.0
|
CG
|
C:ASP10
|
4.8
|
40.0
|
1.0
|
CA
|
C:GLY208
|
4.8
|
24.0
|
1.0
|
CA
|
C:GLY12
|
4.8
|
28.8
|
1.0
|
CG
|
C:ASP206
|
4.9
|
58.1
|
1.0
|
O
|
C:HOH514
|
4.9
|
38.7
|
1.0
|
CE
|
C:LYS77
|
5.0
|
29.3
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 3wt0
Go back to
Magnesium Binding Sites List in 3wt0
Magnesium binding site 4 out
of 4 in the Crystal Structure Analysis of Cell Division Protein
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure Analysis of Cell Division Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg401
b:33.6
occ:1.00
|
O1B
|
D:ATP400
|
1.9
|
29.1
|
1.0
|
O1G
|
D:ATP400
|
2.0
|
37.9
|
1.0
|
O
|
D:HOH506
|
2.0
|
25.5
|
1.0
|
O
|
D:HOH710
|
2.1
|
24.6
|
1.0
|
O
|
D:HOH523
|
2.2
|
29.8
|
1.0
|
O
|
D:HOH507
|
2.2
|
27.3
|
1.0
|
PB
|
D:ATP400
|
3.2
|
30.0
|
1.0
|
PG
|
D:ATP400
|
3.3
|
25.8
|
1.0
|
O
|
D:HOH541
|
3.4
|
38.8
|
1.0
|
O3B
|
D:ATP400
|
3.6
|
32.2
|
1.0
|
O
|
D:HOH553
|
3.8
|
43.8
|
1.0
|
O
|
D:HOH720
|
3.9
|
37.3
|
1.0
|
O3A
|
D:ATP400
|
3.9
|
27.3
|
1.0
|
O
|
D:HOH502
|
3.9
|
21.0
|
1.0
|
NZ
|
D:LYS77
|
4.0
|
26.1
|
1.0
|
OD2
|
D:ASP206
|
4.0
|
57.8
|
1.0
|
O2G
|
D:ATP400
|
4.0
|
29.2
|
1.0
|
O2A
|
D:ATP400
|
4.0
|
57.1
|
1.0
|
OD2
|
D:ASP10
|
4.2
|
35.5
|
1.0
|
OD1
|
D:ASP10
|
4.3
|
40.4
|
1.0
|
O3G
|
D:ATP400
|
4.4
|
32.8
|
1.0
|
O2B
|
D:ATP400
|
4.5
|
26.8
|
1.0
|
NZ
|
D:LYS17
|
4.5
|
36.4
|
1.0
|
PA
|
D:ATP400
|
4.6
|
25.5
|
1.0
|
OD1
|
D:ASP206
|
4.6
|
46.8
|
1.0
|
CG
|
D:ASP206
|
4.7
|
46.2
|
1.0
|
CG
|
D:ASP10
|
4.7
|
34.7
|
1.0
|
CA
|
D:GLY208
|
4.8
|
26.2
|
1.0
|
CA
|
D:GLY12
|
4.8
|
28.1
|
1.0
|
CE
|
D:LYS77
|
4.9
|
27.1
|
1.0
|
|
Reference:
K.Kato,
T.Ishido,
T.Matsui,
M.Yao.
Crystal Structure Analysis of Cell Division Protein To Be Published.
Page generated: Thu Aug 15 13:37:09 2024
|