Magnesium in PDB 6j6q: Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Enzymatic activity of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
All present enzymatic activity of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom:
2.3.2.27;
Other elements in 6j6q:
The structure of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
(pdb code 6j6q). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the
Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom, PDB code: 6j6q:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
Magnesium binding site 1 out
of 6 in 6j6q
Go back to
Magnesium Binding Sites List in 6j6q
Magnesium binding site 1 out
of 6 in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1501
b:54.0
occ:1.00
|
OG
|
C:SER190
|
2.0
|
21.3
|
1.0
|
O1G
|
C:GTP1500
|
2.2
|
35.4
|
1.0
|
O2B
|
C:GTP1500
|
2.2
|
35.4
|
1.0
|
OG1
|
C:THR147
|
2.3
|
18.7
|
1.0
|
O3G
|
C:GTP1500
|
2.8
|
35.4
|
1.0
|
CB
|
C:SER190
|
2.8
|
21.3
|
1.0
|
PG
|
C:GTP1500
|
2.9
|
35.4
|
1.0
|
PB
|
C:GTP1500
|
3.2
|
35.4
|
1.0
|
O3B
|
C:GTP1500
|
3.4
|
35.4
|
1.0
|
CB
|
C:THR147
|
3.6
|
18.7
|
1.0
|
O1B
|
C:GTP1500
|
3.7
|
35.4
|
1.0
|
CA
|
C:SER190
|
3.9
|
21.3
|
1.0
|
N
|
C:SER190
|
3.9
|
21.3
|
1.0
|
N
|
C:THR147
|
4.0
|
18.7
|
1.0
|
OD2
|
C:ASP179
|
4.1
|
23.9
|
1.0
|
O2G
|
C:GTP1500
|
4.3
|
35.4
|
1.0
|
OD1
|
C:ASP179
|
4.3
|
23.9
|
1.0
|
O
|
C:ALA215
|
4.4
|
16.8
|
1.0
|
CA
|
C:THR147
|
4.4
|
18.7
|
1.0
|
CG2
|
C:THR147
|
4.5
|
18.7
|
1.0
|
O3A
|
C:GTP1500
|
4.6
|
35.4
|
1.0
|
CA
|
C:PRO216
|
4.7
|
19.1
|
1.0
|
CB
|
C:LYS146
|
4.7
|
15.4
|
1.0
|
CG
|
C:ASP179
|
4.7
|
23.9
|
1.0
|
O2A
|
C:GTP1500
|
4.7
|
35.4
|
1.0
|
CE
|
C:LYS146
|
4.7
|
15.4
|
1.0
|
OD2
|
C:ASP214
|
4.7
|
18.6
|
1.0
|
N
|
C:GLY217
|
4.9
|
20.4
|
1.0
|
|
Magnesium binding site 2 out
of 6 in 6j6q
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Magnesium Binding Sites List in 6j6q
Magnesium binding site 2 out
of 6 in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg200
b:28.6
occ:1.00
|
OP2
|
B:G1
|
1.5
|
0.1
|
1.0
|
OP1
|
E:G78
|
1.7
|
49.9
|
1.0
|
OP2
|
E:U80
|
2.5
|
55.9
|
1.0
|
P
|
B:G1
|
2.5
|
0.9
|
1.0
|
O3'
|
B:G0
|
2.7
|
77.2
|
1.0
|
P
|
E:G78
|
3.1
|
49.9
|
1.0
|
OP1
|
B:G1
|
3.5
|
0.4
|
1.0
|
O5'
|
B:G1
|
3.7
|
0.3
|
1.0
|
P
|
E:U80
|
3.8
|
55.9
|
1.0
|
O3'
|
E:G77
|
3.9
|
49.5
|
1.0
|
O5'
|
E:G78
|
4.0
|
49.9
|
1.0
|
OP2
|
E:G78
|
4.1
|
49.9
|
1.0
|
O5'
|
E:U80
|
4.1
|
55.9
|
1.0
|
C5'
|
B:G1
|
4.1
|
0.5
|
1.0
|
C3'
|
B:G0
|
4.2
|
78.2
|
1.0
|
OP1
|
E:G60
|
4.3
|
57.3
|
1.0
|
C5'
|
E:G78
|
4.3
|
49.9
|
1.0
|
O2'
|
B:G0
|
4.5
|
79.3
|
1.0
|
O3'
|
E:A79
|
4.7
|
55.2
|
1.0
|
C3'
|
E:A79
|
4.8
|
55.2
|
1.0
|
OP1
|
E:U80
|
4.8
|
55.9
|
1.0
|
C4'
|
B:G0
|
4.9
|
78.7
|
1.0
|
C2'
|
B:G0
|
4.9
|
79.3
|
1.0
|
C5'
|
E:A79
|
5.0
|
55.2
|
1.0
|
C4'
|
E:A79
|
5.0
|
55.2
|
1.0
|
|
Magnesium binding site 3 out
of 6 in 6j6q
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Magnesium Binding Sites List in 6j6q
Magnesium binding site 3 out
of 6 in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg201
b:21.9
occ:1.00
|
OP1
|
E:U80
|
1.7
|
55.9
|
1.0
|
OP1
|
E:A59
|
2.1
|
61.9
|
1.0
|
OP2
|
E:G60
|
2.1
|
57.3
|
1.0
|
P
|
E:A59
|
2.9
|
61.9
|
1.0
|
OP2
|
E:A59
|
3.0
|
61.9
|
1.0
|
P
|
E:U80
|
3.1
|
55.9
|
1.0
|
P
|
E:G60
|
3.2
|
57.3
|
1.0
|
O5'
|
E:A59
|
3.6
|
61.9
|
1.0
|
OP1
|
E:G60
|
3.6
|
57.3
|
1.0
|
OP2
|
E:U80
|
3.8
|
55.9
|
1.0
|
O5'
|
E:U80
|
4.0
|
55.9
|
1.0
|
O3'
|
E:A79
|
4.0
|
55.2
|
1.0
|
O5'
|
E:G60
|
4.0
|
57.3
|
1.0
|
O3'
|
E:C58
|
4.3
|
77.0
|
1.0
|
C5'
|
E:G60
|
4.3
|
57.3
|
1.0
|
C5'
|
E:U80
|
4.3
|
55.9
|
1.0
|
O2'
|
B:A70
|
4.4
|
0.1
|
1.0
|
O3'
|
E:A59
|
4.5
|
61.9
|
1.0
|
O6
|
E:G52
|
4.8
|
57.2
|
1.0
|
N7
|
E:G52
|
4.9
|
57.2
|
1.0
|
C3'
|
E:A59
|
4.9
|
61.9
|
1.0
|
C5'
|
E:A59
|
4.9
|
61.9
|
1.0
|
|
Magnesium binding site 4 out
of 6 in 6j6q
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Magnesium Binding Sites List in 6j6q
Magnesium binding site 4 out
of 6 in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg202
b:21.4
occ:1.00
|
OP2
|
E:G81
|
2.0
|
65.7
|
1.0
|
P
|
E:G81
|
3.5
|
65.7
|
1.0
|
O5'
|
E:G81
|
4.0
|
65.7
|
1.0
|
OP2
|
E:G77
|
4.1
|
49.5
|
1.0
|
OP2
|
E:A62
|
4.2
|
53.8
|
1.0
|
OP2
|
E:G78
|
4.3
|
49.9
|
1.0
|
O3'
|
E:U80
|
4.3
|
55.9
|
1.0
|
OP1
|
E:G81
|
4.4
|
65.7
|
1.0
|
N7
|
E:G78
|
4.5
|
49.9
|
1.0
|
C5'
|
E:G77
|
4.5
|
49.5
|
1.0
|
N7
|
E:G77
|
4.6
|
49.5
|
1.0
|
OP2
|
E:C61
|
4.7
|
52.4
|
1.0
|
OP1
|
E:A62
|
4.7
|
53.8
|
1.0
|
C8
|
E:G77
|
4.8
|
49.5
|
1.0
|
C8
|
E:G78
|
5.0
|
49.9
|
1.0
|
|
Magnesium binding site 5 out
of 6 in 6j6q
Go back to
Magnesium Binding Sites List in 6j6q
Magnesium binding site 5 out
of 6 in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg203
b:24.2
occ:1.00
|
OP1
|
E:G81
|
2.4
|
65.7
|
1.0
|
P
|
E:G81
|
3.8
|
65.7
|
1.0
|
O6
|
E:G63
|
4.1
|
47.7
|
1.0
|
N7
|
E:G81
|
4.2
|
65.7
|
1.0
|
OP2
|
E:A82
|
4.2
|
47.7
|
1.0
|
C8
|
E:G81
|
4.3
|
65.7
|
1.0
|
N7
|
E:A82
|
4.3
|
47.7
|
1.0
|
OP2
|
E:G81
|
4.4
|
65.7
|
1.0
|
O5'
|
E:G81
|
4.5
|
65.7
|
1.0
|
C2'
|
E:U80
|
4.7
|
55.9
|
1.0
|
O3'
|
E:U80
|
4.9
|
55.9
|
1.0
|
N7
|
E:A62
|
4.9
|
53.8
|
1.0
|
C3'
|
E:U80
|
5.0
|
55.9
|
1.0
|
N6
|
E:A82
|
5.0
|
47.7
|
1.0
|
|
Magnesium binding site 6 out
of 6 in 6j6q
Go back to
Magnesium Binding Sites List in 6j6q
Magnesium binding site 6 out
of 6 in the Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Cryo-Em Structure of the Yeast B*-B2 Complex at An Average Resolution of 3.7 Angstrom within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg204
b:23.1
occ:1.00
|
OP1
|
E:G77
|
1.6
|
49.5
|
1.0
|
OP1
|
E:C61
|
1.8
|
52.4
|
1.0
|
P
|
E:G77
|
2.9
|
49.5
|
1.0
|
P
|
E:C61
|
3.2
|
52.4
|
1.0
|
NE2
|
A:GLN748
|
3.2
|
35.9
|
1.0
|
O5'
|
E:G77
|
3.3
|
49.5
|
1.0
|
O3'
|
E:G60
|
3.7
|
57.3
|
1.0
|
O5'
|
E:C61
|
3.8
|
52.4
|
1.0
|
OP2
|
E:G77
|
3.8
|
49.5
|
1.0
|
O3'
|
E:A76
|
4.1
|
47.7
|
1.0
|
CD
|
A:GLN748
|
4.3
|
35.9
|
1.0
|
OP2
|
E:C61
|
4.4
|
52.4
|
1.0
|
C5'
|
E:G77
|
4.4
|
49.5
|
1.0
|
C5'
|
E:C61
|
4.9
|
52.4
|
1.0
|
CG
|
A:GLN748
|
5.0
|
35.9
|
1.0
|
|
Reference:
R.Wan,
R.Bai,
C.Yan,
J.Lei,
Y.Shi.
Structures of the Catalytically Activated Yeast Spliceosome Reveal the Mechanism of Branching. Cell V. 177 339 2019.
ISSN: ISSN 1097-4172
PubMed: 30879786
DOI: 10.1016/J.CELL.2019.02.006
Page generated: Tue Oct 1 04:38:31 2024
|