Magnesium in PDB 6tiu: Drosophila Gtp-Tubulin Y222F Mutant
Protein crystallography data
The structure of Drosophila Gtp-Tubulin Y222F Mutant, PDB code: 6tiu
was solved by
B.Gigant,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.00 /
3.57
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
65.97,
126.35,
249.79,
90,
90,
90
|
R / Rfree (%)
|
22.1 /
24.4
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Drosophila Gtp-Tubulin Y222F Mutant
(pdb code 6tiu). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Drosophila Gtp-Tubulin Y222F Mutant, PDB code: 6tiu:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 6tiu
Go back to
Magnesium Binding Sites List in 6tiu
Magnesium binding site 1 out
of 4 in the Drosophila Gtp-Tubulin Y222F Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Drosophila Gtp-Tubulin Y222F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg502
b:95.4
occ:1.00
|
O1G
|
A:GTP501
|
2.1
|
89.1
|
1.0
|
O1B
|
A:GTP501
|
2.3
|
83.0
|
1.0
|
PG
|
A:GTP501
|
3.2
|
87.7
|
1.0
|
OE1
|
A:GLU71
|
3.4
|
98.0
|
1.0
|
PB
|
A:GTP501
|
3.4
|
81.9
|
1.0
|
O3B
|
A:GTP501
|
3.7
|
87.7
|
1.0
|
OD2
|
A:ASP69
|
3.7
|
86.5
|
1.0
|
O2G
|
A:GTP501
|
3.8
|
90.7
|
1.0
|
OD1
|
A:ASP69
|
3.9
|
88.3
|
1.0
|
O3A
|
A:GTP501
|
4.0
|
82.4
|
1.0
|
NZ
|
B:LYS252
|
4.1
|
106.8
|
1.0
|
CB
|
A:GLN11
|
4.1
|
80.2
|
1.0
|
OD2
|
A:ASP98
|
4.1
|
90.8
|
1.0
|
CG
|
A:ASP69
|
4.2
|
88.9
|
1.0
|
N
|
A:GLN11
|
4.4
|
79.3
|
1.0
|
NE2
|
A:GLN11
|
4.5
|
98.1
|
1.0
|
CB
|
A:ASP98
|
4.5
|
91.7
|
1.0
|
O3G
|
A:GTP501
|
4.6
|
83.9
|
1.0
|
CD
|
A:GLU71
|
4.6
|
112.9
|
1.0
|
O1A
|
A:GTP501
|
4.8
|
84.5
|
1.0
|
CG
|
A:ASP98
|
4.8
|
92.1
|
1.0
|
O2B
|
A:GTP501
|
4.8
|
80.2
|
1.0
|
CB
|
A:GLU71
|
4.8
|
99.3
|
1.0
|
CA
|
A:GLN11
|
4.9
|
79.4
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 6tiu
Go back to
Magnesium Binding Sites List in 6tiu
Magnesium binding site 2 out
of 4 in the Drosophila Gtp-Tubulin Y222F Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Drosophila Gtp-Tubulin Y222F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg502
b:80.9
occ:0.50
|
O1B
|
B:GTP501
|
2.8
|
81.9
|
0.5
|
CB
|
B:GLN11
|
3.0
|
94.3
|
1.0
|
O1G
|
B:GTP501
|
3.4
|
87.7
|
0.5
|
OG1
|
B:THR72
|
3.5
|
128.2
|
1.0
|
O2G
|
B:GTP501
|
3.8
|
89.0
|
0.5
|
CG
|
B:GLN11
|
3.9
|
117.2
|
1.0
|
CA
|
B:GLN11
|
3.9
|
91.8
|
1.0
|
N
|
B:GLN11
|
4.0
|
90.6
|
1.0
|
O2A
|
B:GDP503
|
4.0
|
70.1
|
0.5
|
OE1
|
B:GLN11
|
4.1
|
131.8
|
1.0
|
PG
|
B:GTP501
|
4.1
|
86.1
|
0.5
|
OD2
|
B:ASP67
|
4.1
|
109.3
|
1.0
|
PB
|
B:GTP501
|
4.2
|
80.7
|
0.5
|
OE1
|
B:GLU69
|
4.2
|
118.1
|
1.0
|
CD
|
B:GLN11
|
4.5
|
137.2
|
1.0
|
O3B
|
B:GTP501
|
4.5
|
86.2
|
0.5
|
CB
|
B:THR72
|
4.9
|
127.6
|
1.0
|
O1A
|
B:GDP503
|
4.9
|
72.0
|
0.5
|
OD1
|
B:ASP67
|
4.9
|
103.2
|
1.0
|
PA
|
B:GDP503
|
4.9
|
70.5
|
0.5
|
O3A
|
B:GTP501
|
4.9
|
81.3
|
0.5
|
O1A
|
B:GTP501
|
4.9
|
83.8
|
0.5
|
CG
|
B:ASP67
|
5.0
|
105.0
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 6tiu
Go back to
Magnesium Binding Sites List in 6tiu
Magnesium binding site 3 out
of 4 in the Drosophila Gtp-Tubulin Y222F Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Drosophila Gtp-Tubulin Y222F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg601
b:94.2
occ:1.00
|
O1G
|
C:GTP600
|
2.1
|
90.4
|
1.0
|
O1B
|
C:GTP600
|
2.3
|
89.3
|
1.0
|
PG
|
C:GTP600
|
3.2
|
88.1
|
1.0
|
OE2
|
C:GLU71
|
3.4
|
141.8
|
1.0
|
PB
|
C:GTP600
|
3.5
|
86.8
|
1.0
|
OD2
|
C:ASP69
|
3.6
|
93.7
|
1.0
|
O3B
|
C:GTP600
|
3.6
|
89.2
|
1.0
|
O2G
|
C:GTP600
|
3.6
|
86.0
|
1.0
|
OD1
|
C:ASP69
|
3.7
|
90.0
|
1.0
|
CD
|
C:GLU71
|
3.7
|
132.2
|
1.0
|
OE1
|
C:GLU71
|
3.8
|
133.3
|
1.0
|
OD2
|
C:ASP98
|
4.1
|
91.3
|
1.0
|
O3A
|
C:GTP600
|
4.1
|
92.5
|
1.0
|
CG
|
C:ASP69
|
4.1
|
90.5
|
1.0
|
NZ
|
D:LYS252
|
4.1
|
99.2
|
1.0
|
CB
|
C:GLN11
|
4.3
|
90.0
|
1.0
|
CB
|
C:ASP98
|
4.3
|
91.1
|
1.0
|
N
|
C:GLN11
|
4.5
|
88.3
|
1.0
|
O3G
|
C:GTP600
|
4.6
|
85.4
|
1.0
|
CB
|
C:GLU71
|
4.6
|
99.7
|
1.0
|
CG
|
C:ASP98
|
4.6
|
91.6
|
1.0
|
NE2
|
C:GLN11
|
4.7
|
94.8
|
1.0
|
CG
|
C:GLU71
|
4.8
|
109.2
|
1.0
|
O2B
|
C:GTP600
|
4.8
|
88.7
|
1.0
|
CA
|
C:GLN11
|
4.9
|
88.5
|
1.0
|
OG1
|
C:THR145
|
5.0
|
85.8
|
1.0
|
O1A
|
C:GTP600
|
5.0
|
100.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 6tiu
Go back to
Magnesium Binding Sites List in 6tiu
Magnesium binding site 4 out
of 4 in the Drosophila Gtp-Tubulin Y222F Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Drosophila Gtp-Tubulin Y222F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg502
b:80.9
occ:1.00
|
O1B
|
D:GTP501
|
2.8
|
85.3
|
1.0
|
CB
|
D:GLN11
|
2.8
|
95.8
|
1.0
|
O1G
|
D:GTP501
|
3.2
|
91.2
|
1.0
|
N
|
D:GLN11
|
3.5
|
92.8
|
1.0
|
CA
|
D:GLN11
|
3.6
|
94.1
|
1.0
|
OE1
|
D:GLN11
|
3.7
|
137.2
|
1.0
|
O2G
|
D:GTP501
|
3.7
|
92.2
|
1.0
|
PG
|
D:GTP501
|
3.9
|
89.5
|
1.0
|
CG
|
D:GLN11
|
3.9
|
119.1
|
1.0
|
PB
|
D:GTP501
|
3.9
|
84.0
|
1.0
|
OG1
|
D:THR72
|
4.0
|
119.4
|
1.0
|
OD2
|
D:ASP67
|
4.2
|
102.4
|
1.0
|
O3A
|
D:GTP501
|
4.2
|
84.7
|
1.0
|
O1A
|
D:GTP501
|
4.2
|
87.5
|
1.0
|
CD
|
D:GLN11
|
4.2
|
139.0
|
1.0
|
O3B
|
D:GTP501
|
4.3
|
89.5
|
1.0
|
OD1
|
D:ASP67
|
4.4
|
98.5
|
1.0
|
C
|
D:GLY10
|
4.6
|
94.0
|
1.0
|
OE1
|
D:GLU69
|
4.6
|
143.7
|
1.0
|
CG
|
D:ASP67
|
4.7
|
100.1
|
1.0
|
PA
|
D:GTP501
|
4.8
|
87.5
|
1.0
|
|
Reference:
R.Ayukawa,
S.Iwata,
H.Imai,
S.Kamimura,
M.Hayashi,
K.X.Ngo,
I.Minoura,
S.Uchimura,
T.Makino,
M.Shirouzu,
H.Shigematsu,
K.Sekimoto,
B.Gigant,
E.Muto.
Gtp-Dependent Formation of Straight Tubulin Oligomers Leads to Microtubule Nucleation J.Cell Biol. 2021.
ISSN: ESSN 1540-8140
DOI: 10.1083/JCB.202007033
Page generated: Tue Oct 1 18:59:13 2024
|