Magnesium in PDB 7k9y: Gsi-Iic Rt Template-Switching Complex (Twinned)
Protein crystallography data
The structure of Gsi-Iic Rt Template-Switching Complex (Twinned), PDB code: 7k9y
was solved by
J.L.Stamos,
A.M.Lentzsch,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.79 /
3.20
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
179.38,
107.415,
71.973,
90,
113.65,
90
|
R / Rfree (%)
|
27.1 /
32.4
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Gsi-Iic Rt Template-Switching Complex (Twinned)
(pdb code 7k9y). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Gsi-Iic Rt Template-Switching Complex (Twinned), PDB code: 7k9y:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 7k9y
Go back to
Magnesium Binding Sites List in 7k9y
Magnesium binding site 1 out
of 2 in the Gsi-Iic Rt Template-Switching Complex (Twinned)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Gsi-Iic Rt Template-Switching Complex (Twinned) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg503
b:139.2
occ:1.00
|
OD1
|
A:ASP138
|
2.1
|
147.9
|
1.0
|
O1B
|
A:DTP501
|
2.1
|
125.7
|
1.0
|
O1G
|
A:DTP501
|
2.1
|
132.2
|
1.0
|
OD2
|
A:ASP223
|
2.1
|
126.6
|
1.0
|
O
|
A:LEU139
|
2.1
|
142.7
|
1.0
|
O1A
|
A:DTP501
|
2.1
|
121.9
|
1.0
|
CG
|
A:ASP138
|
3.1
|
150.4
|
1.0
|
CG
|
A:ASP223
|
3.3
|
123.4
|
1.0
|
C
|
A:LEU139
|
3.3
|
139.8
|
1.0
|
PB
|
A:DTP501
|
3.3
|
118.4
|
1.0
|
PG
|
A:DTP501
|
3.4
|
124.4
|
1.0
|
PA
|
A:DTP501
|
3.4
|
115.5
|
1.0
|
OD2
|
A:ASP138
|
3.5
|
152.3
|
1.0
|
N
|
A:LEU139
|
3.7
|
138.7
|
1.0
|
O3A
|
A:DTP501
|
3.7
|
114.5
|
1.0
|
O3B
|
A:DTP501
|
3.8
|
117.3
|
1.0
|
O2G
|
A:DTP501
|
3.9
|
122.3
|
1.0
|
OD1
|
A:ASP223
|
4.0
|
128.2
|
1.0
|
CA
|
A:LEU139
|
4.0
|
139.8
|
1.0
|
C5'
|
A:DTP501
|
4.1
|
105.4
|
1.0
|
O5'
|
A:DTP501
|
4.3
|
108.9
|
1.0
|
CB
|
A:PHE142
|
4.3
|
91.6
|
1.0
|
CB
|
A:ASP223
|
4.4
|
118.9
|
1.0
|
N
|
A:LYS141
|
4.4
|
114.6
|
1.0
|
N
|
A:GLU140
|
4.4
|
136.1
|
1.0
|
CB
|
A:ASP138
|
4.4
|
151.3
|
1.0
|
N
|
A:PHE142
|
4.4
|
99.0
|
1.0
|
C
|
A:ASP138
|
4.4
|
147.4
|
1.0
|
O2A
|
A:DTP501
|
4.6
|
118.0
|
1.0
|
O3G
|
A:DTP501
|
4.6
|
130.2
|
1.0
|
CB
|
A:LEU139
|
4.6
|
139.8
|
1.0
|
O2B
|
A:DTP501
|
4.6
|
118.4
|
1.0
|
CA
|
A:GLU140
|
4.7
|
132.8
|
1.0
|
C
|
A:GLU140
|
4.8
|
127.7
|
1.0
|
CA
|
A:ASP138
|
4.8
|
150.9
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 7k9y
Go back to
Magnesium Binding Sites List in 7k9y
Magnesium binding site 2 out
of 2 in the Gsi-Iic Rt Template-Switching Complex (Twinned)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Gsi-Iic Rt Template-Switching Complex (Twinned) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg503
b:131.1
occ:1.00
|
O1B
|
D:DTP501
|
2.1
|
116.7
|
1.0
|
OD1
|
D:ASP138
|
2.1
|
142.1
|
1.0
|
O1G
|
D:DTP501
|
2.1
|
119.2
|
1.0
|
OD2
|
D:ASP223
|
2.1
|
128.8
|
1.0
|
O
|
D:LEU139
|
2.1
|
141.7
|
1.0
|
O2A
|
D:DTP501
|
2.1
|
124.3
|
1.0
|
CG
|
D:ASP138
|
3.1
|
146.2
|
1.0
|
PG
|
D:DTP501
|
3.2
|
113.4
|
1.0
|
PB
|
D:DTP501
|
3.2
|
110.0
|
1.0
|
CG
|
D:ASP223
|
3.3
|
125.6
|
1.0
|
C
|
D:LEU139
|
3.3
|
143.7
|
1.0
|
PA
|
D:DTP501
|
3.4
|
121.9
|
1.0
|
OD2
|
D:ASP138
|
3.5
|
144.2
|
1.0
|
O3B
|
D:DTP501
|
3.6
|
112.1
|
1.0
|
O2G
|
D:DTP501
|
3.6
|
111.6
|
1.0
|
O3A
|
D:DTP501
|
3.6
|
115.3
|
1.0
|
N
|
D:LEU139
|
3.6
|
148.1
|
1.0
|
OD1
|
D:ASP223
|
4.0
|
125.0
|
1.0
|
CA
|
D:LEU139
|
4.0
|
146.3
|
1.0
|
CB
|
D:PHE142
|
4.2
|
115.2
|
1.0
|
CB
|
D:ASP223
|
4.3
|
122.9
|
1.0
|
O1A
|
D:DTP501
|
4.3
|
119.5
|
1.0
|
N
|
D:PHE142
|
4.4
|
119.7
|
1.0
|
N
|
D:GLU140
|
4.4
|
140.6
|
1.0
|
N
|
D:LYS141
|
4.4
|
127.1
|
1.0
|
CB
|
D:ASP138
|
4.4
|
147.3
|
1.0
|
C
|
D:ASP138
|
4.4
|
147.4
|
1.0
|
O5'
|
D:DTP501
|
4.5
|
118.5
|
1.0
|
C5'
|
D:DTP501
|
4.5
|
121.0
|
1.0
|
O3G
|
D:DTP501
|
4.5
|
112.7
|
1.0
|
O2B
|
D:DTP501
|
4.6
|
112.5
|
1.0
|
CB
|
D:LEU139
|
4.6
|
149.1
|
1.0
|
CA
|
D:GLU140
|
4.7
|
137.1
|
1.0
|
C
|
D:GLU140
|
4.8
|
133.3
|
1.0
|
CA
|
D:ASP138
|
4.8
|
147.2
|
1.0
|
CA
|
D:PHE142
|
4.9
|
119.5
|
1.0
|
NZ
|
D:LYS258
|
5.0
|
166.6
|
1.0
|
|
Reference:
A.M.Lentzsch,
J.L.Stamos,
J.Yao,
R.Russell,
A.M.Lambowitz.
Structural Basis For Template Switching By A Group II Intron-Encoded Non-Ltr-Retroelement Reverse Transcriptase. J.Biol.Chem. 00971 2021.
ISSN: ESSN 1083-351X
PubMed: 34280434
DOI: 10.1016/J.JBC.2021.100971
Page generated: Wed Oct 2 22:09:23 2024
|