Magnesium in PDB 2nvq: Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp
Enzymatic activity of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp
All present enzymatic activity of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp:
2.7.7.6;
Protein crystallography data
The structure of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp, PDB code: 2nvq
was solved by
D.Wang,
D.A.Bushnell,
K.D.Westover,
C.D.Kaplan,
R.D.Kornberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.45 /
2.90
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
170.646,
222.760,
195.281,
90.00,
101.31,
90.00
|
R / Rfree (%)
|
22.9 /
28.3
|
Other elements in 2nvq:
The structure of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp
(pdb code 2nvq). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the
Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp, PDB code: 2nvq:
Jump to Magnesium binding site number:
1;
2;
3;
Magnesium binding site 1 out
of 3 in 2nvq
Go back to
Magnesium Binding Sites List in 2nvq
Magnesium binding site 1 out
of 3 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg2001
b:46.3
occ:1.00
|
OD2
|
A:ASP485
|
2.1
|
51.1
|
1.0
|
OD1
|
A:ASP485
|
2.2
|
54.5
|
1.0
|
CG
|
A:ASP485
|
2.2
|
49.9
|
1.0
|
OD2
|
A:ASP483
|
2.3
|
53.2
|
1.0
|
OD1
|
A:ASP481
|
2.5
|
59.2
|
1.0
|
C3'
|
R:A10
|
2.9
|
39.3
|
1.0
|
C4'
|
R:A10
|
3.2
|
36.9
|
1.0
|
CG
|
A:ASP483
|
3.2
|
54.7
|
1.0
|
C5'
|
R:A10
|
3.5
|
31.2
|
1.0
|
OD1
|
A:ASP483
|
3.5
|
59.1
|
1.0
|
CB
|
A:ASP485
|
3.6
|
48.1
|
1.0
|
C5'
|
T:DUT29
|
3.6
|
74.7
|
0.3
|
O2A
|
T:DUT29
|
3.7
|
77.4
|
0.3
|
CG
|
A:ASP481
|
3.8
|
57.4
|
1.0
|
O1G
|
T:DUT29
|
3.8
|
98.7
|
0.7
|
O2'
|
R:A10
|
3.9
|
44.1
|
1.0
|
C2'
|
R:A10
|
4.0
|
39.5
|
1.0
|
O5'
|
T:DUT29
|
4.0
|
76.8
|
0.3
|
N
|
A:ASP485
|
4.1
|
47.8
|
1.0
|
CA
|
A:ASP485
|
4.2
|
47.3
|
1.0
|
NH2
|
A:ARG446
|
4.2
|
57.2
|
1.0
|
PA
|
T:DUT29
|
4.3
|
77.5
|
0.3
|
O3G
|
T:DUT29
|
4.4
|
98.8
|
0.7
|
C4'
|
T:DUT29
|
4.5
|
73.1
|
0.3
|
N
|
A:ASP481
|
4.5
|
51.8
|
1.0
|
O1A
|
T:DUT29
|
4.6
|
77.4
|
0.3
|
OD2
|
A:ASP481
|
4.6
|
63.8
|
1.0
|
O4'
|
R:A10
|
4.6
|
36.4
|
1.0
|
CB
|
A:ASP483
|
4.7
|
50.4
|
1.0
|
O5'
|
R:A10
|
4.7
|
24.9
|
1.0
|
CB
|
A:ASP481
|
4.7
|
53.3
|
1.0
|
PG
|
T:DUT29
|
4.8
|
97.9
|
0.7
|
C
|
A:ASP483
|
4.8
|
48.4
|
1.0
|
N
|
A:ASP483
|
4.9
|
49.4
|
1.0
|
CA
|
A:ASP481
|
4.9
|
52.4
|
1.0
|
C
|
A:GLY484
|
4.9
|
47.5
|
1.0
|
O
|
A:ASP483
|
5.0
|
47.7
|
1.0
|
N
|
A:GLY484
|
5.0
|
49.1
|
1.0
|
|
Magnesium binding site 2 out
of 3 in 2nvq
Go back to
Magnesium Binding Sites List in 2nvq
Magnesium binding site 2 out
of 3 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg2002
b:43.6
occ:0.66
|
O2B
|
T:DUT29
|
2.3
|
94.2
|
0.7
|
O4'
|
T:DUT29
|
2.8
|
77.7
|
0.7
|
C4'
|
T:DUT29
|
3.2
|
80.4
|
0.7
|
PB
|
T:DUT29
|
3.4
|
95.2
|
0.7
|
OD2
|
A:ASP481
|
3.5
|
63.8
|
1.0
|
C1'
|
T:DUT29
|
3.5
|
77.6
|
0.7
|
O1G
|
T:DUT29
|
3.7
|
80.3
|
0.3
|
O1B
|
T:DUT29
|
3.9
|
94.4
|
0.7
|
O3'
|
T:DUT29
|
4.0
|
76.4
|
0.7
|
O3A
|
T:DUT29
|
4.1
|
91.1
|
0.7
|
C3'
|
T:DUT29
|
4.2
|
78.9
|
0.7
|
C5'
|
T:DUT29
|
4.4
|
87.0
|
0.7
|
N1
|
T:DUT29
|
4.4
|
77.5
|
0.7
|
O5'
|
T:DUT29
|
4.6
|
95.5
|
0.7
|
C2'
|
T:DUT29
|
4.6
|
78.6
|
0.7
|
NH2
|
B:ARG1020
|
4.7
|
68.2
|
1.0
|
OE1
|
B:GLU836
|
4.7
|
69.9
|
1.0
|
CG
|
A:ASP481
|
4.7
|
57.4
|
1.0
|
O3B
|
T:DUT29
|
4.8
|
96.7
|
0.7
|
O2
|
T:DUT29
|
4.8
|
77.0
|
0.7
|
PG
|
T:DUT29
|
4.8
|
79.7
|
0.3
|
O1G
|
T:DUT29
|
4.9
|
98.7
|
0.7
|
C2
|
T:DUT29
|
5.0
|
77.2
|
0.7
|
|
Magnesium binding site 3 out
of 3 in 2nvq
Go back to
Magnesium Binding Sites List in 2nvq
Magnesium binding site 3 out
of 3 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with 2'Dutp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg2002
b:33.1
occ:0.34
|
O3G
|
T:DUT29
|
2.1
|
78.6
|
0.3
|
O1G
|
T:DUT29
|
2.4
|
80.3
|
0.3
|
OD2
|
B:ASP837
|
2.6
|
67.1
|
1.0
|
PG
|
T:DUT29
|
2.7
|
79.7
|
0.3
|
OD1
|
A:ASP483
|
2.8
|
59.1
|
1.0
|
O3B
|
T:DUT29
|
3.5
|
79.4
|
0.3
|
NH2
|
B:ARG1020
|
3.5
|
68.2
|
1.0
|
CG
|
B:ASP837
|
3.6
|
65.8
|
1.0
|
O3B
|
T:DUT29
|
3.8
|
96.7
|
0.7
|
CZ
|
B:ARG1020
|
3.9
|
64.6
|
1.0
|
O1B
|
T:DUT29
|
4.0
|
94.4
|
0.7
|
OD2
|
A:ASP481
|
4.0
|
63.8
|
1.0
|
O2B
|
T:DUT29
|
4.0
|
94.2
|
0.7
|
CG
|
A:ASP483
|
4.0
|
54.7
|
1.0
|
PB
|
T:DUT29
|
4.1
|
95.2
|
0.7
|
O2G
|
T:DUT29
|
4.3
|
79.6
|
0.3
|
OD1
|
B:ASP837
|
4.3
|
70.3
|
1.0
|
CG
|
A:ASP481
|
4.4
|
57.4
|
1.0
|
NH1
|
B:ARG1020
|
4.4
|
63.0
|
1.0
|
OD1
|
A:ASP481
|
4.4
|
59.2
|
1.0
|
O1B
|
T:DUT29
|
4.4
|
78.6
|
0.3
|
CB
|
B:ASP837
|
4.5
|
60.7
|
1.0
|
NE
|
B:ARG1020
|
4.5
|
62.7
|
1.0
|
O1G
|
T:DUT29
|
4.5
|
98.7
|
0.7
|
CB
|
A:ASP483
|
4.6
|
50.4
|
1.0
|
PG
|
T:DUT29
|
4.6
|
97.9
|
0.7
|
O2A
|
T:DUT29
|
4.6
|
77.4
|
0.3
|
O3G
|
T:DUT29
|
4.7
|
98.8
|
0.7
|
PB
|
T:DUT29
|
4.7
|
78.8
|
0.3
|
|
Reference:
D.Wang,
D.A.Bushnell,
K.D.Westover,
C.D.Kaplan,
R.D.Kornberg.
Structural Basis of Transcription: Role of the Trigger Loop in Substrate Specificity and Catalysis Cell(Cambridge,Mass.) V. 127 941 2006.
ISSN: ISSN 0092-8674
PubMed: 17129781
DOI: 10.1016/J.CELL.2006.11.023
Page generated: Wed Aug 14 00:56:41 2024
|