Magnesium in PDB 8v7i: Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S
Enzymatic activity of Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S
All present enzymatic activity of Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S:
2.7.7.7;
Protein crystallography data
The structure of Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S, PDB code: 8v7i
was solved by
C.Chang,
Y.Gao,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.67 /
1.72
|
Space group
|
P 61
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.547,
98.547,
81.894,
90,
90,
120
|
R / Rfree (%)
|
21.2 /
23.3
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S
(pdb code 8v7i). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S, PDB code: 8v7i:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 8v7i
Go back to
Magnesium Binding Sites List in 8v7i
Magnesium binding site 1 out
of 2 in the Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:23.6
occ:0.80
|
OD1
|
A:ASP13
|
2.0
|
35.5
|
1.0
|
O1B
|
A:DTP503
|
2.1
|
23.5
|
0.8
|
O2G
|
A:DTP503
|
2.1
|
29.3
|
0.8
|
OD2
|
A:ASP115
|
2.2
|
38.9
|
0.8
|
O1A
|
A:DTP503
|
2.2
|
30.6
|
0.8
|
O
|
A:MET14
|
2.2
|
28.9
|
1.0
|
CG
|
A:ASP13
|
2.9
|
26.9
|
1.0
|
PB
|
A:DTP503
|
3.1
|
31.1
|
0.8
|
OD2
|
A:ASP13
|
3.2
|
52.7
|
1.0
|
PG
|
A:DTP503
|
3.3
|
30.7
|
0.8
|
C
|
A:MET14
|
3.3
|
18.6
|
1.0
|
PA
|
A:DTP503
|
3.3
|
38.1
|
0.8
|
O3A
|
A:DTP503
|
3.4
|
34.4
|
0.8
|
CG
|
A:ASP115
|
3.4
|
30.3
|
0.8
|
MG
|
A:MG502
|
3.4
|
26.7
|
0.4
|
O3B
|
A:DTP503
|
3.5
|
27.9
|
0.8
|
OD2
|
A:ASP115
|
3.7
|
25.2
|
0.2
|
C5'
|
A:DTP503
|
3.8
|
33.3
|
0.8
|
CG
|
A:ASP115
|
3.9
|
28.0
|
0.2
|
O3G
|
A:DTP503
|
3.9
|
24.0
|
0.8
|
N
|
A:MET14
|
4.0
|
16.3
|
1.0
|
OD1
|
A:ASP115
|
4.1
|
31.5
|
0.8
|
O
|
A:HOH601
|
4.1
|
34.8
|
0.4
|
O5'
|
A:DTP503
|
4.1
|
33.4
|
0.8
|
NZ
|
A:LYS231
|
4.1
|
27.4
|
1.0
|
N
|
A:ASP15
|
4.2
|
21.2
|
1.0
|
CA
|
A:MET14
|
4.2
|
14.1
|
1.0
|
CB
|
A:ASP13
|
4.2
|
21.2
|
1.0
|
N
|
A:CYS16
|
4.2
|
22.9
|
1.0
|
C
|
A:ASP13
|
4.3
|
17.4
|
1.0
|
CB
|
A:ASP115
|
4.3
|
20.9
|
0.2
|
CA
|
A:ASP15
|
4.4
|
20.8
|
1.0
|
CB
|
A:ASP115
|
4.4
|
20.7
|
0.8
|
OD1
|
A:ASP115
|
4.4
|
29.1
|
0.2
|
C
|
A:ASP15
|
4.5
|
20.7
|
1.0
|
O1G
|
A:DTP503
|
4.5
|
30.6
|
0.8
|
O2B
|
A:DTP503
|
4.5
|
25.2
|
0.8
|
O
|
A:ASP115
|
4.5
|
23.6
|
1.0
|
O2A
|
A:DTP503
|
4.5
|
38.8
|
0.8
|
CA
|
A:ASP13
|
4.6
|
17.6
|
1.0
|
N
|
A:PHE17
|
4.7
|
14.8
|
1.0
|
O
|
A:ASP13
|
4.8
|
17.4
|
1.0
|
CB
|
A:MET14
|
4.9
|
22.9
|
1.0
|
CA
|
A:CYS16
|
5.0
|
20.0
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 8v7i
Go back to
Magnesium Binding Sites List in 8v7i
Magnesium binding site 2 out
of 2 in the Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg502
b:26.7
occ:0.40
|
O1A
|
A:DTP503
|
2.2
|
30.6
|
0.8
|
OD1
|
A:ASP115
|
2.3
|
31.5
|
0.8
|
O
|
A:HOH601
|
2.4
|
34.8
|
0.4
|
OD1
|
A:ASP115
|
2.4
|
29.1
|
0.2
|
C3'
|
P:CAR9
|
2.6
|
33.7
|
0.3
|
OD2
|
A:ASP13
|
2.7
|
52.7
|
1.0
|
OE2
|
A:GLU116
|
2.7
|
40.6
|
1.0
|
O3'
|
P:CAR9
|
2.7
|
32.1
|
0.3
|
OD2
|
A:ASP115
|
2.8
|
38.9
|
0.8
|
CG
|
A:ASP115
|
2.8
|
30.3
|
0.8
|
CG
|
A:ASP115
|
3.1
|
28.0
|
0.2
|
CD
|
A:GLU116
|
3.4
|
36.8
|
1.0
|
CG
|
A:ASP13
|
3.4
|
26.9
|
1.0
|
OD2
|
A:ASP115
|
3.4
|
25.2
|
0.2
|
PA
|
A:DTP503
|
3.4
|
38.1
|
0.8
|
MG
|
A:MG501
|
3.4
|
23.6
|
0.8
|
C4'
|
P:CAR9
|
3.5
|
34.3
|
0.3
|
CG
|
A:GLU116
|
3.6
|
46.7
|
1.0
|
CB
|
A:GLU116
|
3.7
|
29.2
|
1.0
|
OD1
|
A:ASP13
|
3.8
|
35.5
|
1.0
|
C5'
|
P:CAR9
|
3.8
|
32.7
|
0.3
|
C2'
|
P:CAR9
|
3.9
|
35.0
|
0.3
|
O
|
A:ASP115
|
3.9
|
23.6
|
1.0
|
O5'
|
A:DTP503
|
3.9
|
33.4
|
0.8
|
O2A
|
A:DTP503
|
4.0
|
38.8
|
0.8
|
C5'
|
A:DTP503
|
4.0
|
33.3
|
0.8
|
O3'
|
P:CAR9
|
4.1
|
37.9
|
0.7
|
OG
|
A:SER113
|
4.1
|
24.8
|
1.0
|
C
|
A:ASP115
|
4.1
|
25.8
|
1.0
|
CB
|
A:ASP115
|
4.1
|
20.9
|
0.2
|
CB
|
A:ASP115
|
4.2
|
20.7
|
0.8
|
OE1
|
A:GLU116
|
4.3
|
37.4
|
1.0
|
CB
|
A:ASP13
|
4.4
|
21.2
|
1.0
|
O2'
|
P:CAR9
|
4.4
|
36.4
|
0.3
|
N
|
A:GLU116
|
4.4
|
20.7
|
1.0
|
CA
|
A:GLU116
|
4.5
|
20.6
|
1.0
|
O2G
|
A:DTP503
|
4.6
|
29.3
|
0.8
|
CA
|
A:ASP115
|
4.7
|
20.1
|
0.2
|
CA
|
A:ASP115
|
4.7
|
20.0
|
0.8
|
O3A
|
A:DTP503
|
4.7
|
34.4
|
0.8
|
O1B
|
A:DTP503
|
4.8
|
23.5
|
0.8
|
O4'
|
P:CAR9
|
4.8
|
29.8
|
0.3
|
C3'
|
P:CAR9
|
4.8
|
36.5
|
0.7
|
C1'
|
P:CAR9
|
4.9
|
32.1
|
0.3
|
CA
|
A:ASP13
|
5.0
|
17.6
|
1.0
|
NZ
|
A:LYS224
|
5.0
|
34.9
|
1.0
|
|
Reference:
C.Chang,
Y.Gao.
Human Dna Polymerase Eta-Dna-Arac-Ended Primer Ternary Complex:Reaction with 1 Mm MG2+ For 1800S To Be Published.
Page generated: Fri Oct 4 22:01:22 2024
|