Magnesium in PDB 5kfp: Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S
Enzymatic activity of Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S
All present enzymatic activity of Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S:
2.7.7.7;
Protein crystallography data
The structure of Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S, PDB code: 5kfp
was solved by
Y.Gao,
W.Yang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.84 /
1.70
|
Space group
|
P 61
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.540,
98.540,
81.590,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
17.7 /
22.1
|
Other elements in 5kfp:
The structure of Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S
(pdb code 5kfp). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the
Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S, PDB code: 5kfp:
Jump to Magnesium binding site number:
1;
2;
3;
Magnesium binding site 1 out
of 3 in 5kfp
Go back to
Magnesium Binding Sites List in 5kfp
Magnesium binding site 1 out
of 3 in the Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S
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 Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:26.4
occ:0.45
|
OD2
|
A:ASP13
|
2.0
|
26.5
|
0.6
|
O
|
A:HOH680
|
2.2
|
36.1
|
1.0
|
OE2
|
A:GLU116
|
2.3
|
39.7
|
1.0
|
OP1
|
P:AS9
|
2.4
|
27.3
|
0.3
|
OD1
|
A:ASP115
|
2.4
|
26.2
|
1.0
|
O2A
|
A:STP508
|
2.5
|
27.4
|
0.6
|
O3'
|
P:DT8
|
2.6
|
33.4
|
0.7
|
O3'
|
P:DT8
|
2.7
|
32.7
|
0.3
|
MG
|
A:MG504
|
2.8
|
26.5
|
0.5
|
OD1
|
A:ASP13
|
2.8
|
18.3
|
0.4
|
P
|
P:AS9
|
3.0
|
32.2
|
0.3
|
CG
|
A:ASP13
|
3.0
|
22.8
|
0.6
|
CD
|
A:GLU116
|
3.1
|
35.8
|
1.0
|
CG
|
A:ASP13
|
3.3
|
22.0
|
0.4
|
CG
|
A:ASP115
|
3.3
|
24.0
|
1.0
|
OD2
|
A:ASP13
|
3.4
|
21.8
|
0.4
|
OD1
|
A:ASP13
|
3.4
|
20.2
|
0.6
|
C3'
|
P:DT8
|
3.5
|
38.5
|
0.7
|
OD2
|
A:ASP115
|
3.6
|
23.1
|
1.0
|
MG
|
A:MG503
|
3.6
|
21.9
|
0.8
|
CA
|
A:CA502
|
3.6
|
21.9
|
0.1
|
PA
|
A:STP508
|
3.7
|
30.4
|
0.6
|
CB
|
A:GLU116
|
3.8
|
29.0
|
1.0
|
C3'
|
P:DT8
|
3.9
|
36.9
|
0.3
|
OE1
|
A:GLU116
|
3.9
|
34.0
|
1.0
|
OG
|
A:SER113
|
3.9
|
23.4
|
1.0
|
CG
|
A:GLU116
|
3.9
|
24.2
|
1.0
|
C4'
|
P:DT8
|
4.1
|
36.8
|
0.3
|
O5'
|
A:STP508
|
4.1
|
28.8
|
0.6
|
C4'
|
P:DT8
|
4.1
|
37.3
|
0.7
|
O5'
|
P:AS9
|
4.2
|
28.8
|
0.3
|
C5'
|
P:DT8
|
4.3
|
36.5
|
0.3
|
CB
|
A:ASP13
|
4.3
|
15.6
|
0.6
|
NZ
|
A:LYS224
|
4.3
|
27.8
|
0.7
|
O5
|
A:DPO509
|
4.3
|
20.8
|
0.3
|
C5'
|
A:STP508
|
4.3
|
28.4
|
0.6
|
C5'
|
P:AS9
|
4.4
|
28.2
|
0.3
|
CB
|
A:ASP13
|
4.4
|
15.7
|
0.4
|
S2P
|
P:AS9
|
4.4
|
41.1
|
0.3
|
O1
|
A:DPO509
|
4.4
|
23.3
|
0.3
|
C5'
|
P:DT8
|
4.4
|
36.7
|
0.7
|
O
|
P:HOH105
|
4.5
|
43.5
|
1.0
|
O1G
|
A:STP508
|
4.5
|
20.9
|
0.6
|
O
|
A:ASP115
|
4.5
|
16.8
|
1.0
|
C
|
A:ASP115
|
4.5
|
20.4
|
1.0
|
S1A
|
A:STP508
|
4.5
|
42.8
|
0.6
|
N
|
A:GLU116
|
4.6
|
14.6
|
1.0
|
O
|
A:HOH797
|
4.7
|
33.0
|
1.0
|
CB
|
A:ASP115
|
4.7
|
18.8
|
1.0
|
C2'
|
P:DT8
|
4.8
|
36.4
|
0.7
|
CA
|
A:GLU116
|
4.8
|
19.8
|
1.0
|
O1B
|
A:STP508
|
4.9
|
18.8
|
0.6
|
CA
|
A:ASP13
|
4.9
|
16.3
|
0.4
|
O
|
A:HOH618
|
4.9
|
39.0
|
1.0
|
CA
|
A:ASP13
|
5.0
|
16.2
|
0.6
|
C2'
|
P:DT8
|
5.0
|
34.5
|
0.3
|
|
Magnesium binding site 2 out
of 3 in 5kfp
Go back to
Magnesium Binding Sites List in 5kfp
Magnesium binding site 2 out
of 3 in the Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S
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 Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg503
b:21.9
occ:0.85
|
CA
|
A:CA502
|
0.0
|
21.9
|
0.1
|
O1
|
A:DPO509
|
1.6
|
23.3
|
0.3
|
O5
|
A:DPO509
|
1.9
|
20.8
|
0.3
|
O1B
|
A:STP508
|
2.0
|
18.8
|
0.6
|
O1G
|
A:STP508
|
2.0
|
20.9
|
0.6
|
OD2
|
A:ASP115
|
2.2
|
23.1
|
1.0
|
OD1
|
A:ASP13
|
2.2
|
20.2
|
0.6
|
OD1
|
A:ASP13
|
2.2
|
18.3
|
0.4
|
O
|
A:MET14
|
2.3
|
18.2
|
1.0
|
O2A
|
A:STP508
|
2.4
|
27.4
|
0.6
|
OP1
|
P:AS9
|
2.4
|
27.3
|
0.3
|
P1
|
A:DPO509
|
3.0
|
24.4
|
0.3
|
PB
|
A:STP508
|
3.1
|
24.5
|
0.6
|
P2
|
A:DPO509
|
3.1
|
24.4
|
0.3
|
MG
|
A:MG504
|
3.1
|
26.5
|
0.5
|
CG
|
A:ASP13
|
3.2
|
22.0
|
0.4
|
CG
|
A:ASP13
|
3.2
|
22.8
|
0.6
|
PG
|
A:STP508
|
3.2
|
23.8
|
0.6
|
CG
|
A:ASP115
|
3.3
|
24.0
|
1.0
|
C
|
A:MET14
|
3.4
|
17.8
|
1.0
|
O4
|
A:DPO509
|
3.4
|
24.8
|
0.3
|
PA
|
A:STP508
|
3.5
|
30.4
|
0.6
|
O3B
|
A:STP508
|
3.6
|
25.1
|
0.6
|
MG
|
A:MG501
|
3.6
|
26.4
|
0.5
|
OD2
|
A:ASP13
|
3.6
|
21.8
|
0.4
|
O3A
|
A:STP508
|
3.6
|
30.9
|
0.6
|
OD2
|
A:ASP13
|
3.6
|
26.5
|
0.6
|
OD1
|
A:ASP115
|
3.7
|
26.2
|
1.0
|
O2
|
A:DPO509
|
3.8
|
30.7
|
0.3
|
P
|
P:AS9
|
3.8
|
32.2
|
0.3
|
O7
|
A:DPO509
|
3.8
|
22.1
|
0.3
|
O2G
|
A:STP508
|
3.9
|
22.4
|
0.6
|
C5'
|
A:STP508
|
3.9
|
28.4
|
0.6
|
N
|
A:MET14
|
4.0
|
13.9
|
1.0
|
O3
|
A:DPO509
|
4.0
|
23.2
|
0.3
|
C5'
|
P:AS9
|
4.0
|
28.2
|
0.3
|
NZ
|
A:LYS231
|
4.1
|
21.2
|
1.0
|
O5'
|
P:AS9
|
4.1
|
28.8
|
0.3
|
N
|
A:CYS16
|
4.2
|
16.4
|
1.0
|
O5'
|
A:STP508
|
4.2
|
28.8
|
0.6
|
CA
|
A:MET14
|
4.2
|
13.9
|
1.0
|
C
|
A:ASP13
|
4.2
|
12.8
|
1.0
|
O6
|
A:DPO509
|
4.3
|
27.4
|
0.3
|
N
|
A:ASP15
|
4.3
|
13.8
|
1.0
|
O2B
|
A:STP508
|
4.4
|
18.2
|
0.6
|
O
|
A:HOH797
|
4.4
|
33.0
|
1.0
|
CA
|
A:ASP15
|
4.4
|
15.0
|
1.0
|
O3G
|
A:STP508
|
4.4
|
27.6
|
0.6
|
CB
|
A:ASP13
|
4.5
|
15.6
|
0.6
|
C
|
A:ASP15
|
4.5
|
18.8
|
1.0
|
CB
|
A:ASP13
|
4.5
|
15.7
|
0.4
|
CB
|
A:ASP115
|
4.5
|
18.8
|
1.0
|
O
|
A:HOH680
|
4.5
|
36.1
|
1.0
|
N
|
A:PHE17
|
4.6
|
13.8
|
1.0
|
O
|
A:ASP13
|
4.6
|
14.2
|
1.0
|
CB
|
A:MET14
|
4.7
|
15.3
|
1.0
|
CA
|
A:ASP13
|
4.8
|
16.3
|
0.4
|
CA
|
A:ASP13
|
4.8
|
16.2
|
0.6
|
O3'
|
P:DT8
|
4.8
|
32.7
|
0.3
|
CB
|
A:PHE17
|
4.8
|
14.3
|
1.0
|
O
|
A:ASP115
|
4.8
|
16.8
|
1.0
|
CA
|
A:CYS16
|
5.0
|
15.7
|
1.0
|
|
Magnesium binding site 3 out
of 3 in 5kfp
Go back to
Magnesium Binding Sites List in 5kfp
Magnesium binding site 3 out
of 3 in the Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Human Dna Polymerase Eta-Dna Ternary Complex with Sp-Datp-Alpha-S: Reaction with 20 Mm MG2+ For 600S within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg504
b:26.5
occ:0.45
|
O
|
A:HOH797
|
2.0
|
33.0
|
1.0
|
O
|
A:HOH680
|
2.0
|
36.1
|
1.0
|
O2A
|
A:STP508
|
2.0
|
27.4
|
0.6
|
OP1
|
P:AS9
|
2.1
|
27.3
|
0.3
|
OD2
|
A:ASP13
|
2.4
|
21.8
|
0.4
|
O5
|
A:DPO509
|
2.5
|
20.8
|
0.3
|
O1G
|
A:STP508
|
2.5
|
20.9
|
0.6
|
MG
|
A:MG501
|
2.8
|
26.4
|
0.5
|
OD2
|
A:ASP13
|
2.9
|
26.5
|
0.6
|
OD1
|
A:ASP13
|
2.9
|
20.2
|
0.6
|
P
|
P:AS9
|
3.0
|
32.2
|
0.3
|
PA
|
A:STP508
|
3.1
|
30.4
|
0.6
|
CA
|
A:CA502
|
3.1
|
21.9
|
0.1
|
MG
|
A:MG503
|
3.1
|
21.9
|
0.8
|
CG
|
A:ASP13
|
3.1
|
22.0
|
0.4
|
OD1
|
A:ASP13
|
3.1
|
18.3
|
0.4
|
CG
|
A:ASP13
|
3.2
|
22.8
|
0.6
|
S1A
|
A:STP508
|
3.4
|
42.8
|
0.6
|
S2P
|
P:AS9
|
3.4
|
41.1
|
0.3
|
P2
|
A:DPO509
|
3.6
|
24.4
|
0.3
|
O6
|
A:DPO509
|
3.7
|
27.4
|
0.3
|
PG
|
A:STP508
|
3.7
|
23.8
|
0.6
|
O1
|
A:DPO509
|
3.8
|
23.3
|
0.3
|
O3A
|
A:STP508
|
3.8
|
30.9
|
0.6
|
O3G
|
A:STP508
|
3.8
|
27.6
|
0.6
|
O3'
|
P:DT8
|
3.8
|
32.7
|
0.3
|
O
|
A:HOH618
|
4.0
|
39.0
|
1.0
|
O2
|
A:DPO509
|
4.0
|
30.7
|
0.3
|
P1
|
A:DPO509
|
4.3
|
24.4
|
0.3
|
O4
|
A:DPO509
|
4.3
|
24.8
|
0.3
|
NZ
|
A:LYS224
|
4.3
|
27.8
|
0.7
|
O1B
|
A:STP508
|
4.3
|
18.8
|
0.6
|
O3'
|
P:DT8
|
4.4
|
33.4
|
0.7
|
PB
|
A:STP508
|
4.4
|
24.5
|
0.6
|
O5'
|
P:AS9
|
4.4
|
28.8
|
0.3
|
O5'
|
A:STP508
|
4.4
|
28.8
|
0.6
|
O3B
|
A:STP508
|
4.5
|
25.1
|
0.6
|
C3'
|
P:DT8
|
4.6
|
38.5
|
0.7
|
CB
|
A:ASP13
|
4.6
|
15.6
|
0.6
|
OE2
|
A:GLU116
|
4.6
|
39.7
|
1.0
|
CB
|
A:ASP13
|
4.6
|
15.7
|
0.4
|
OD2
|
A:ASP115
|
4.6
|
23.1
|
1.0
|
OD1
|
A:ASP115
|
4.7
|
26.2
|
1.0
|
O
|
A:HOH606
|
4.7
|
42.3
|
1.0
|
O
|
A:HOH628
|
4.7
|
35.8
|
1.0
|
O7
|
A:DPO509
|
4.8
|
22.1
|
0.3
|
NZ
|
A:LYS231
|
4.8
|
21.2
|
1.0
|
C3'
|
P:DT8
|
4.8
|
36.9
|
0.3
|
O2G
|
A:STP508
|
4.9
|
22.4
|
0.6
|
CE
|
A:LYS231
|
5.0
|
40.8
|
1.0
|
|
Reference:
Y.Gao,
W.Yang.
Capture of A Third MG2+ Is Essential For Catalyzing Dna Synthesis. Science V. 352 1334 2016.
ISSN: ESSN 1095-9203
PubMed: 27284197
DOI: 10.1126/SCIENCE.AAD9633
Page generated: Sun Sep 29 18:57:26 2024
|